peroxidases ( peroksida )

PEROXI DASES 1970 - 1-9~O

PEROXIDASES 1970 ·1980

A SURVEY OF THEIR BIOCHEMICAL AND PHYSIOLOGICAL ROLES IN HIGHER

PLANTS

Thomas GASPAR, Claude PENEL, Trevor THORPE :" ...... and Hubert GREPPIN

UNIVERSITÉ DE GENÈVE - CENTRE DE BOTANIQUE

GENÈVE 1982

Thomas GASPAR

Head Laboratory of Fundamental and Applied Hormonology, Botanical Institute, University of Liège, Belgium, and Lecturer, University of Genève, Switzeriand.

Claude PENEL

Chef de Service, Laboratory of Plant Physiology, and Lecturer, University of Genève, Switzeriand.

Trevor THORPE

Professor of Botany, Department of Biology, University of Calgary, Canada. Past-Chairman of the International Association for Plant Tissue Culture.

Hubert GREPPIN

Professor of Plant Physiology and Ecophysiology, Head Laboratory of Plant Physiology, Past-Chairman Department of Biology Department, Dean Faculty of Sciences, University of Genève, SwÏtzeriand.

1

ACKNOWLEDGEMENTS

It is a pleasure to acknowledge the support of the Centre de Botanique and the Centre Universitaire d'Informatique of Genève, which made this volume possible. The authors express their appreciation to their respective secretary-typists for their cooperation, and particularly to Mrs. Christiane Tschopp for her assistance with the editorial work on the word processing machine BG-lOOO. Thomas Gaspar and Claude Penel thank the University of Genève as weil as the Swiss and Belgian National Science Foundations which facilitated the scientific exchanges between Genève and Liège.

CONTENTS

PART ONE

Chapter 1. INTRODUCTION 3

Chapter 2. CHEMISTRY AND BIOCHEMISTRY OF PEROXIDASES 9

2.1. CHEMICAL STRUCTURE 9

2.\.\. Prosthetic group 10 2.1.2. Protein \1 2.1.3. Compounds 13

2.2. FORMATION OF COMPOUNDS l, II and III AND CATALYTIC REACTIONS 14

2.2.\. 2.2.2.

Reaction mechanisms in presence of H20

2 Reaction mechanisms in absence of H

20

2

17 19

2.3. PARTICULAR PEROXIDASE REACTIONS 21

2.3.1. Types of reactions and substrates 21 2.3.2. IAA degradation 25 2.3.3. 2.3.4.

H20

2 formation and .Iignin biosynthesis

Ethylene biosynthesis 33 44

2.4. TYPES OF PEROXIDASES 48

1

Chapter 3. ISOPEROXIDASES: FACT OR FICTION ? 61

Chapter 4. SUBCELLULAR LOCALIZATION AND BIOSYNTHESIS OF PEROXIDASES 71

4.1. CELLULAR LOCALIZATION OF PEROXIDASES 71

4.1.1. TechnicaI aspects 71 4.1.2. Cellular localization 73

4.2. BIOSYNTHESIS OF PEROXIDASES AND ITS REGULATION 79

4.2.1. De nova synthesis or activation 79 4.2.2. Transcription 80 4.2.3. Translation 81 4.2.4. Post-translational steps and secretion 82

Chapter 5. PHYSIOLOGICAL PROCESSES MEDIATED BY PEROXIDASES 89

5.1. AUXIN CATABOLISM 90

5.1.1. Growth 91 5.1.2. Morpho- and organogenetic processes 97

5.2. LIGNIN FORMATION 101

5.2.1. Growth 101 5.2.2. Ditferentiation, vascularization 102

5.3. DEFENSE MECHANISMS AGAINST PATHOGENS 103

5.4. RESPIRATION 107

5.5. UGHT MEDIATED PROCESSES 108

5.5.1. Peroxidases as pigments 108 5.5.2. Peroxidases and phytochrome 109 5.5.3. Photoperiodic control and flowering 112

!

,-:

Chapter 6. PRACTICAL APPLICATIONS OF PEROXIDASES 123

Chapter 7. CONCLUDING REMARKS AND PROSPECTS 131

PART TWO

REFERENCES 137

AUTHOR INDEX 255

ORGANISMIC INDEX 303

SUBJECT INDEX 313

. j

i

ccc

ABBREVIATIONS

ACC

C l, Il, III

CCP

con A

2,4-0

DAB

DCP

DHF

EDTA

EGTA

Fe J+ P

Fe 2+ P

GA

GC-ECO

GLC-ECD

1-aminocycJopropane- 1-carboxylic acid

Compound l, Il, III

2-chloro-ethyltrimethylammonium chloride

cytochrome c peroxidase

concanavalin A

2,4-dichlorophenoxyacetic acid

3,3'-diaminobenzidine

2,4-dich lorophenol

dihydroxyfumarate

ethylenediamine tetraacetic acid

ethylene glycol-bis (2-aminoethylether) N,N'-tetraacetic acid

ferriperoxidase

ferroperoxidase

gibberellic acid

gas chromatography - electron capture detection

gas liquid chromatography - electron capture detection

HRP

IAA

Kapp

KMBA

NAD

SAM

horseradish peroxidase

indole-3-acetic acid

apparent dissociation constant

cx-keto-y-methylthiopropionaldehyde

nicotinamide adenine dinucleotide

S-adenosyl-methionine

3NO ~HVd

CHAPTER 1

INTRODUCTION

Peroxidases (donor : H20

2 oxidoreductase; EC. 1.11.1.7) are

enzymes, whose primary function is to oxidize molecules at the expense of hydrogen peroxide. Since they are widely distributed in living organisms, and show dramatic color-product formation as a resultof their catalytic effect, these enzymes have been among the most extensively investigated since the beginnings of enzymology (1459).

Perhaps the earliest report on peroxidase activity was in 1855 by Schonbein, who observed that certain organic compounds could be oxidized by dilute solutions of hydrogen peroxide in the presence of substances occurring in plants and animais (Saunders et al., 1964). The name peroxidase was first given by Linossier, who in 1898 isolated it from pus.

Studies carried out in the period up to 1918 showed that peroxidase activity was widely found in plants. Relatively pure peroxidase was also obtained during this period. It was also shown that the peroxidase system could oxidize pyrogallol, gallic acid and certain amines (Saunders et al., 1964).

During the period 1918-1931, the enzyme was purified, and the determination of its activity was carried out by assessing the oxidation of pyrogallol to purpurogallin. In 1931 it was shown that peroxidase was a hematin (Saunders et al., 1964). The last 50 years has seen an exponential increase in the number of people working on peroxidase, so much so that during the 1970-1980 period sorne 1600 plus references have appeared on the enzyme (see bibliography Section).

The phenomenon of peroxidase multiplicity has been known for many years but it was not until the development of the zymogram technique by Hunter and Market (1957) that the occurence of isoperoxidases came under extensive investigation. It is now an established

4 PEROXIDASES 1970/1980

fact that most enzymes exist in multiple molecular forms. Tt is further acknowledged that a large amount of the variation detected in isozyme studies has a genetic base, thus rendering isozymes as useful markers in the analysis of gene functions and metabolic regulation in growing and differentiating cells and tissues (1159).

Peroxidase is probably the enzyme appearing under the largest number of isoforms (up to 42 in horseradish, ref. 584) in plants examined.. This fact makes them suspect as native molecules as such (see Chapter 3) and automatically renders studies involving isoperoxidases doubtful as to their real significance. The problem is further complicated by the obligatory or non-obligatory enzyme intermediate Compounds l, II and III and the relative specificity towards a wide range of hydrogen donors such as phenolic substances, cytochrome c, nitrite, leuco-dyes, ascorbic acid, indole amines, and certain inorganic ions, especially the iodide ion. Moreover, besides peroxidasic oxidation of electron donor molecules, various reactions have been found to be catalyzed by peroxidase. These are aerobic oxidations of dihydroxyfumarate (Swedin and Theorell, 1940; Chance, 1952), IAA (see Section 2.3.2), triose reductone (Yamazaki et al., 1956), NADH (Akazawa and Conn, 1958; Yokota and Yamazaki, 1965) and naphthohydroquinone (Klapper and Hackett, 1963), hydroxylation of aromatic molecules (Mason et al., 1957; Buhler and Mason, 1961), formation of ethylene (see Section 2.3.4), halogenation (Morrison et al., 1970; Hager et al., 1970) and antimicrobial activity (see Section 5.3).

If the cornmon feature of these reactions appears to be an involvement of HzOz' from the point of view of function, however, peroxidase is rather similar to oxidase, the name of which is now used in a narrow sense for electron transfer oxidases. The name 'oxygenase' is restricted to enzymes that catalyze the incorporation of atmospheric oxygen into substrate molecules (Hayaishi, 1974). Thus based on the acceptor specificity and by analysis of final reaction products, the distinction between electron transfer oxidase, oxygenase and peroxidase appear to be weil established (1459).

Reaction of mixed types suchas monooxygenase (mixed function oxidase by Mason's (1957, 1965) terminology) and peroxidase-oxidase have been reported. If peroxide is an intermediate product of Oz reduction it might be said that in many cases peroxide metabolism is involved as a part of the overall oxygen metabolism. Detailed analysis of the mechanism of Oz metabolism have revealed that three types of reactions are correlated in complicated ways as indicated below :

5 INTRODUCTION

oxidase (electron transfer)

I~ oxygenase .. ~ peroxidase

The recently established idea of the oxyferroperoxidase structure for so-called Compound III would make it easy to relate the function of peroxidase- with those of electron transfer oxidase and oxygenase (1459, see Chapter 2).

Peroxidases have the capacity to catalyze a large number of biochemical reactions. In plants and in animais, they apparently fulfil many different functions and certainly we are far from knowing everything about them. Their ubiquity and their biochemical versatility explain why peroxidases are the subject of so many publications. But despite the fact that peroxidases are among the most studied enzymes, or, perhaps due to the great number and the diversity of the articles devoted to their study, there has been no comprehensive review, since Saunders, Holmes-Siedle and Stark published their book in 1964. That book essentially dealt with the biochemical aspects of peroxidases. Since that time, peroxidases have been extensively examined in biological and physiological studies.

One major objective of the present book is to gather in one place the references of articles concerned with peroxidases that have appeared during the last ten years. These references coyer ail the aspects of peroxidase research (biochemistry, physiology, genetics, histo- and cytochemistry). This bibliographic matter mainly concerns higher plant peroxidases, but there are also a few hundred references dealing with animal or human biology. These latter are of general interest. Three indexes (authors names, subjects and organisms) facilitate the search of references. The second major objective is to critically review what is known about the enzyme. Thus, the reader will also find several chapters covering all aspects of the peroxidase story.

It is our hope that this book, which is written by plant physiologists from a physiological viewpoint, will be of value to all people working with peroxidases. For those unfamiliar with the enzyme we hope that our synthesis of the available information will lead to a clearer understanding of peroxidase, the most extensively examined enzyme in plants.


REFERENCES

For numbered references in the text, see bibliographical section

AKAZA\VA, T.; CONN, E.E. 1958. The oxidation of reduced pyridine nucleotides by peroxidase. J. BIOL. CHEM. 232: 403415.

BUHLER, D.R.; MASON, H.S. 1961. Hydroxylation catalyzed by peroxidase. ARCH. BIOCHEM. BIOPHYS. 92: 424-437.

CHANCE, B. 1952. Oxidase and peroxidase reactions in the presence of dihydroxymaleic acid. J. BIOL. CHEM. 197: 577-589.

HAGER, L.P.; THOMAS, J.A.; MORRIS, D.R. 1970. Studies on the relationship ofchloroperoxidase - halide and chloroperoxidase hydrogen peroxide complexes to the mechanism of the halogenation reaction. In 'BIOCHEMISTRY OF THE PHAGOCYTIC PROCESS'. Schultz, J. (Ed.). North-Holland Publ., Amsterdam, pp. 67-87.

HAYAISHI, O. 1974. General properties and biological functions of oxygenases. In 'MOLECULAR MECHANISMS OF OXYGEN ACTIVATION'. Hayaishi, O. (Ed.). Academie Press, New York, pp. 1-28.

HUNTER, R.L.; MARKERT, C.L. 1957. Histochemical demonstration of enzymes separated by zone electrophoresis in starch gels. SCIENCE 125: 1294-1295.

KLAPPER, M.H.; HACKETT, D.P. 1963. The oxidatic activity of horseradish peroxidase. II. Participation of ferroperoxidase. J. BIOL. CHEM. 238: 3743-3749.

MASON, H.S. 1957. Mechanisms of oxygen metabolism. ADV. ENZYMOL. 19: 79-233.

MASON, H.S. 1965. Oxidases. ANN. REV. BIOCHEM. 34: 595-634. MASON, H.S.; ONOPRYENKO, 1.; BUHLER, D.R. 1957.

Hydroxylation: The activation of oxygen by peroxidase. BIOCHIM. BIOPHYS. ACTA 24: 225-226.

MORRISON, M.; BA YSE, G.; DANNER, D.J. 1970. The role of mammalian peroxidase in iodination reactions. In 'BIOCHEMISTRY OF THE PHAGOCYTIC PROCESS'. Schultz, J. (Ed.). North-Holland Publ., Amsterdam, pp. 51-66.

INTRODUCTION 7

SAUNDERS, Re.; HOLMES-SIEDLE, A.G.; STARK, RP. 1964. Peroxidase. The properties and uses of a versatile enzyme and sorne related catalysts. Butterworths, London, 271 p.

SWEDIN, B.; THEORELL, H. 1940. Dioximaleic acid oxidase action of peroxidases. NATURE 145: 71-72.

y AMAZAKI, 1.; FUJINAGA, K.; TAKEHARA, 1.; TAKAHASHI, H. 1956. Aerobic oxidation of triose reductone by crystalline tumip peroxidase. J. BIOCHEM. 43: 377-386. '

YOKOTA, K.; YAMAZAKI, 1. 1965. The activity of the horseradish : peroxidase compound Ill. BIOCHEM. BIOPHYS. RES. COMM. 18: 38-53.

CHAPTER 2

CHEMISTRY AND BIOCHEMISTRY OF PEROXIDASES

Today, much is known about the chemistry and biochemistry of peroxidases. As a matter of fact, much more has been definitively determined in this area than on any other aspect of the peroxidase story. In this chapter, we will discuss the chemical structure, the formation of various peroxidase compounds and their catalytic mechanisms, specifie peroxidase reactions and final1y the ditferent types of peroxidases known to date.

2.1. CHEMICAL STRUCTURE

Peroxidases and isoperoxidases have been purified from ditferent plant material and it appears that they do not significantly ditfer in size (from 40,000 to 50,000 daltons), absorption spectrum and activity (Theorell, 1942; Jermyn and Thomas, 1954; Paul, 1958; Klapper and Hackett, 1965). They are formed (Fig. 1a) from a colourless glycoprotein combined to a brown-red ferriporphyrin (Fig. 1b).

10 PEROXIDASES 19701 J 980

o Peroxidase 1

1 1

Protohaematin IX: GlycoproteinLr 1

Fe 3+ Protoporphyrin :IX

® ,r CH2

CH

CH~CH2H3C

H3C CH3

CH2/

CH2 \. /C~

HO "'0

Protohaematin JX

Fig. J. a. Structure of peroxidase. b. Structure of protohaematin IX.

2.1.1. Prosthetic group

The prosthetic groups of horseradish peroxidase (HRP), Japanese radish peroxidase, cytochrome c peroxidase (CCP) and chloroperoxidase are known to be ferriprotoporphyrin IX (Fig. lb). Its spectrum gives the same general picture, with bands ex, 13 and y, as that of other metallic phorphyrins (Nari and Penon, 1968; 432). The heme groups in animal peroxidases are much more tightly bound to the protein that are the hemes in plant peroxidases (1459).

CH2 "CH2/C

cf 'OH

BIOCHEMISTRy Il

2.1.2. Protein

Little was known about the chemical structure of peroxidases until relatively recently. Amino acid analysis have been carried out for isoenzyme preparations of HRP (Shannon et a/., 1966; 1208), for two isoenzyme preparations of Japanese radish peroxidase (Morita and Kameda, 1959; Shimizu and Morita, 1966), two peroxidases of wheat (619), five peroxidases from turnip and horseradish (1425) and eight isoperoxidases of tobacco (680). About 300 residues of 16 amino acids were found together with +/- 20% sugars (glucose, galactose, mannose, arabinose, xylose, fucose, hexosamine).

The first complete amino acid sequence of a plant peroxidase was obtained by Welinder (1424). A refined analysis of the quantitatively dominant HRP peroxidase C among the isoperoxidases of horseradish root (l424a) indicates that it consists of a hemin prosthetic group, 2Ca2

+ and 308 amino acid residues, including 4 disulfide bridges, in a single polypeptide chain that carries 8 neutral carbohydrate sidechains. The molecular weight of the polypeptide chain is 33,890. Assuming an average carbohydrate composition of (G le NAc)2' Man

3,

Fuc, Xyl for each carbohydrate chain, the molecular weight of native HRP C is close to 44,000. The complete amino acid sequence of turnip peroxidase P

7 has since also been determined and compared to

that of HRP C (853, 854). The calcium binding by two HRP isoenzymes has been confirmed

and already has been related to its properties (530, 966). Calcium particularly contributes to maintaining the structural conformation of the protein as indicated by the effects of calcium removal (by guanidine hydrochloride and EDTA) on the thermal stability of the protein. Calcium-free HRP isoenzyme C, but not isoenzyme A, can be reconstituted upon addition of calcium and regains enzymatic activity. Free calcium readily exchanges with isoenzyme C, but only to a small extent with isoenzyme A (530). ft must be mentioned that sorne isoperoxidases apparently do not contain carbohydrate (679, 1054).

ft appears on the other hand that sorne soluble (Shannon et al., 1966; 904) and cell wall bound (283) peroxidases might contain hydroxyproline.


The conformation of different HRP and tumip isoenzymes has been investigated by means of circular dichroism, and it has been suggested that although the active sites are similar, sorne small differences did exist (Strickland et al., 1968; 624), and that the isoenzymes differed in amino acid and carbohydrate compositions (Mazza et al., 1968; 851). Since their secondary structures appeared to be very similar, it was suggested that only a few amino acid residues around the heme group goVem the spectral characteristics. It was shown that peroxidases from tumip and an isoperoxidase from horseradish contain highly homologous peptides, thought to be located in proximal and distal positions of the heme iron (1425).

The environment surrounding the heme of CCP has been found to be hydrophobie (Asakura and Yonetani, 1969). This is possibly the case with ail plant peroxidases. The hydrophobie structure of the heme environment of myoglobin and hemoglobin was disclosed by X-ray analyses.

The influence of the heme environment on physicochemical properties and catalytic activity is clearly manifested in the peroxidase isoenzymes from tumip. Thus the most basic isoperoxidase P differs

7 from the other tumip enzymes in possessing low peroxidase and high 'oxidase' activities towards IAA (627, 852). The electronic structure of the heme· and the tertiary structure of the heme crevice are essentially the same in the acidic tumip peroxidases, PI and Pz, and isoperoxidase P

7 (1438). The postulated difference between PI and P

7, i.e., that a

carboxyl group is replaced by a histidine residue as distal groups of the proteins, is in agreement with the amino-acid content of the proteins (1102).

A possibility that the fifth coordination position in HRP is occupied by an imidazole group of the protein was suggested by several workers (Brill and Williams, 1961; Nakamura et al., 1963; 1208, 1474a). By elaborate experiments using '4NO, Yonetani (1474a) concluded that the fifth ligand of the heme iron in CCP and HRP may be the imidazole group of a histidine residue and that the unpaired electron of NO sits in the sixth coordination position although it is considerably delocalized to the heme iron and the proximal nitrogen in these NO compounds of ferrous peroxidases.

13BJOCHEMISTRY

2.1.3. Compounds

Peroxidase reacts with numerous substances (cyanide, fluoride, etc.) and fonus with them stable complexes which can be detected by spectrophotometry. The enzyme can also be reduced by strong reductants such as. hydrosulfite, methylviologen semiquinone, etc. : the ferroperoxidase fonu is then generated. It shows a low affinity towards cyanide (Keilin and Hartree, 1955) but a high specificity in binding carbon monoxide to fonu the photodissociable carboxyferroperoxidase. Cyanide and CO then were often used during peroxidase catalyzed reactions in order to detect the ferri- and/or the ferroperoxidase forms. Ferroperoxidase also reacts with oxygen to form oxyferroperoxidase.

~

1 E ~ '\:J~u 100

1 ~

-1

1 ID

1

1

1 UJ

E ~ 1

l

TT

-T E U

T 5 ~

-E W

400 500 600 700 wovelenglh (nm)

Fig 2. Absorption spectra offerriperoxidase (P) and Compounds 1, II and III (from 432).

Plant peroxidases generally fonu with peroxides three types of compounds called Compounds J, II and III, which have characteristic absorption spectra (Fig. 2). The state of the knowledge of the electronic structure of the heme in these three compounds has been given by Yamazaki (1459) and further studied by several authors (106, 225a, 625, 628, 633, 678, 1002, 1004).


2.2. FORMATION OF COMPOUNDS l, Il AND III

AND CATALYTIC REACTIONS

Peroxidase Compounds 1 and II are formed in the presence of low peroxide concentration only. The green Compound l appears first. It is further transformed in Compound II through reduction by an electron donor. The following reactions have been confirmed for the peroxidase catalysis of its characteristic one-electron oxidation of donor molecules :

Peroxidase + HzOz ----+~ Compound l

Compound 1 + AH2

~ Compound II + AH"

Compound II + AH ~ peroxidase + AH"z

2AH- ~ A + AH (or AH - AH)z

Compounds 1 and Il are thus considered to be obligatory enzyme intermediates in an overall peroxidase reaction regenerating the original ferriperoxidase.

Judged by the hyperfine structure of the electron spin resonance spectra, the free radicals derived from several donor molecules in the above reactions were judged to be free in solution (Yamazaki et al., 1960; Piette et al., 1961). These free radicals are very reactive, and their reactions will result in a variety of peroxidase functions (see below).

Compound III has been identified as a product formed in the presence of excess HzOz (Keilin and Hartree, 1951; George, 1953). It was shown by Chance (1952) and George (1953) that Compound III was formed from the reaction of Compound Il and H

Z02" On the other

hand, Yokota and Yamazaki (1965) observed that Compound III disappeared in the presence of electron donors and acceptors to give ferriperoxidase, which led them to propose the fol1owing reactions :

15BIOCHEMISTRY

+e Compound III ------........ Fep3+ + H2 ° 2(Fe 2+0 ) (2H+)

P 2

or -e

Compound III -------+. Fep3+ + °2

(Fe 3+0-) p 2

This makes Compound III a hybrid between the complexes ferroperoxidase-oxygen and ferriperoxidase-superoxide anion.

This also would mean that Compound III can react with ferroperoxidase and Compound II (Bjorksten, 1968; 1033) :

C III + ferroperoxidase --+ 2 ferriperoxidase + H20 2

CIII+CII ----+ 2 ferriperoxidase + 02

An oxyferroperoxidase structure has been suggested for peroxidase Compound III (Mason, 1957, 1958; George, 1952; Yamazaki & Piette, 1963; Yamazaki el al., 1965). This idea, however, was not generally accepted since reduced peroxidase was thought to be oxidized to the ferric enzyme without an intermediate similar to Compound III (Theorell, 1947; Harbury, 1957). Recently, the oxyferroperoxidase structure of Compound III has been confirmed on the basis of the following data :

(a) Ferroperoxidase reacted with oxygen to form Compound III, when excess hydrosulfite that reduced Compound III was not present (Yamazaki and Yokota, 1965; Yamazaki el al., 1966; Wittenberg el a/., 1967).

(b) Compound III was formed by photolysis of an aerobic solution of CO-ferroperoxidase (Blumberg et a/., 1968; 1312).

(c) Titrimetric experiments showed that Compound III was at a three equivalent oxidized state above the ferric enzyme (Wittenberg et a/. , 1967; 1312; Yamazaki el a/., 1968).

16 PEROX]DASES 1970/1980

Fig. 3. The live redox states of HRP. The numbers in the circles indicate the effective oxidation number of heme. See Yamazaki (1459) for the oxidation potentials.

Figure 3 shows the relationship between the five redox forms of HRP. Ali these forms can be obtained in fairly stable states under suitable experimental conditions and have been crystallized using a basic HRP preparation, named 'isoenzyme F'. Higher oxidation forms of HRP can be reduced to the ferric enzyme by various electron donars. The most active form is Compound 1. ]t has been shown that nitrous acid (Chance, 1952) and p-aminobenzoic acid (Chance and Ferguson, 1954) reduce Compound ] 100 and 25 times faster than Compound Il. Similar results have been obtained by Cormier and Prichard (1968) with luminol, by Dunford and colleagues with ferrocyanide (532) and iodide (1120, 1122), and by Yamazaki et al. (1 460a) with ascorbic acid and anthranilic acid. The conversion of HRP Compound] to the ferric enzyme without an appreciable formation of Compound II was reported by Bjorksten (117) and Roman and Dunford (1120), using iodide as an electron donor.

HRP Compound III also reacted with various electron donars which are not autoxidizable (Yamazaki et al., 1965; 1312; Yokota and Yamazaki, 1965). Compound III was less reactive with electron donars than Compound Il, while in the absence of such donars Compound II was less stable than Compound III. The stability of Compound Il varied greatly with enzyme preparations, but that of Compound III was almost independent of the purity of the enzyme preparations (13 J2).

17 BIOCHEMISTRy

HRP Compound III was shown to undergo spontaneous decay to the ferric enzyme without detectable intermediates like Compounds 1 and II (Yamazaki el al., 1966; Wittenberg el al., 1312). This might be explained by assuming that the oxidative decomposition of Compound III occurs in the presence of one-eJectron oxidants such as Compounds 1 and II.

Compound III + e- , peroxidase + Oz

Rate constants of the reactions of Compound III with Compounds 1 and II can be measured. However, the release of Oz during the reaction has not been confirmed. For the decomposition of Compound III a mechanism, in which dissociation of Compound III into Compound II and HzOz is rate limiting, was proposed (1312), but this needs further proof.

The reaction of Compound III with electron donors is of particular interest. Undoubtedly, Oz is activated when it combines with ferroperoxidase. It might be reasonable to assume that Compound III is reduced by electron donors via the intermediates Compound 1 and II. As mentioned above, these intermediates are much more active oxidants for the electron donors used so far. Therefore, an ingenious device would be needed to identify the intermediates in the reduction process of Compound III.

The direct conversion from ferrous HRP to Compound II was demonstrated by Noble and Gibson (950).

2.2.1. Reaction mechanisms in presence of HO z z

During the course of peroxidase reactions, oxygen is consumed. This a priori couId be due to two quite different processes :

- a direct interaction of the reduced hemoprotein formed during the reaction with oxygen,


- a reaction with oxygen of intermediary unstable degradation products of the electron donor.

ln the former case, the formation of Compound III during the reactions has to be considered. In the latter one, only Compounds 1 and II would play a role.

The formation of Compound III during the aerobic oxidation of dihydroxyfumarate (DHF) (Swedin and Theorell, 1940; Lemberg and Legge, 1949; Mason, 1958; Yamazaki and Piette, 1963; Yamazaki et al., 1965) and NADH (Yokota and Yamazaki, 1965) catalyzed by the system peroxidase-H

20

2 has been observed. This formation as well as

that of ferroperoxidase might be the result of secondary reactions and Compound III would not be necessarily involved in the 'peroxidation' pathway mediated essentially by Compounds 1 and II.

The transitions C 1 to C II and C II to Fe 3+, coupled with electron donor oxidations, give rise to donor radicals (yamazaki et al., 1960; Ray, 1962; Parups, 1969). The reaction of these reducing radicals with oxygen certainly permits the use of the gas during the peroxidase reactions. This reaction subsequently generates a superoxide radical which itself would oxidize another donor molecule and thereby would contribute to the propagation of a free radicals' chain as illustrated in Figure 4.

-----_ .... ------ , : 1

1 1

1 1

1

1

1 1

1

1 , 1

1

1

1

CN 1

1

1

1

1AH·"'" "'02 1

1 l ' , 1 L ~

Fig. 4. Oxidation mechanism of an e1ectron donor (AHz) by the peroxidase-peroxide system. The enclosed part corresponds to the free radicals's chain propagation (afier Yamazaki, 1958 and Ricard and Nari, 1967).

BIOCHEMISTRY 19

In this mechanism, there would be no reaction of the enzyme with oxygen at any time and the formation of Compound III, as already mentioned above, would be the result of a reaction between Fe 3+ and the superoxide radical.

p

2.2.2. Reaction mechanisms in absence of H 0 2 2

Substances such as hydro- and naphthoquinones (Klapper and Hackett, 1963) and IAA (see 432) can be oxidized by peroxidase in the absence of peroxide being introduced in the reaction mixture. The medium has been suspected of containing peroxide traces from the beginning and more peroxide could be formed later on through autooxidation of electron donors.

Klapper and Hackett (1963) however did not exclude the possibility of a direct reduction of ferriperoxidase into ferroperoxidase by the electron donors and therefore proposed a mechanism of peroxidase oxidation without participation of peroxide (Fig. 5). An analogous mechanism involving ferriperoxidase reduction and the subsequent formation of the reactive oxyferroperoxidase (C III) has been proposed by Ricard and Nari (1966) for IAA oxidation (see below).

c:r" °2Fe~+ «7' ~ Fe~+ '>. COMPOUND /II

{~~1 (~r'~ ~ (FepOJ+)

AH AH 2

A+ Hp2 A+H 0 2

COMPOUND 1/ (Fep0 2+)

Fil? 5. Oxidation mechanism of hydro- and naphthoquinones (alier Klapper and Hackett. (963).


The peroxidase mediated IAA oxidation in the absence of peroxide has also been explained by Fox et al. (1965, 1968) through an interaction of ferriperoxidase with oxygen and IAA in order to form a compound identical to C 1. This C 1 would further generate C II which would oxidize IAA. The following sequence has been proposed :

Fe 3+ + 0 ------+. Fe 3+0 p 2 p 2

Fe 3+0 + IAA -----+. CI p 2

e CI -----.... CIl

C II + IAA -----....... Fe 3+ + IAA" p

This IAA- radical would finally react with oxygen as does the AH in the Yamazaki's scheme (Fig. 4).

The binding ofdifferent hydrogen donars and inhibitors to peroxidase will not be examined here, although it has been studied by several authors (744,1162).

21 BIOCHEMISTRy

2.3. PARTICULAR PEROXIDASE REACTIONS

2.3.1. Types of reactions and substrates

Substrate Product Reference

Oxidation with H 02 2

acetosyringone dimethoxyquinone 1476

2,2'-azino-di- corresponding 217 (3-ethyl-benzthia- azodication zoline-6-sulphonic acid) (ABTS)

benzidine benzidine blue Maehly and Chance (1954)

betacyanin unknown 723

chlorophyllides unknown 840

chlorpromazine semi-quinone free radical 239

crocin unknown 325

N,N-dialkyl- secondary amines + 421a, 422 anilines aldehydes

o-dianisidine bis (3,3'-dimethoxy- Moller and 4-amino)azo-biphenyl Ottolenghi

(1966)

22

dihydroxyphenylalanine

di-isopropyl-Nnitrosamine

ferulic acid

guaiacol

3-hydroxyflavone

indolyl-3acetaldehyde

kaempferol

leuco-malachite green

lignins

pyridoxal

pyrogallol

scopoletin

vanillic acid

PEROXIDASES 1970/1980

dopachrome

hydroxy-N-nitrosamine

unknown

tetraguaiaco1

salicylic acid + phenylglyoxylic acid + benzoic acid

indole-3-carbaldehyde

2,3,4,5,7,4'-penthydroxyflavanone + p-hydroxybenzoic acid

malachite green

corresponding quinones

unknown

purpurogallin

unknown

dehydrovanillic acid

84

349

1036

Maehly and Chance (1954)

1178

1467

573


1476

566


1085

97

23

Oxidation with Oz

dihydroxymaleie aeid (Mnz+)

dithiothreitol

NAD(P)H(Mnz+, ROH)

2,4,6/3,5 pentahydroxyeyclohexane (Mnz+)

phenylaeetaldehyde (Mnz+)

phenylpyruvate (Mnz+, DCP)

2',4,4'-trihydroxyehalcone

4,2',4'-trihydroxy-ehalcone

BIOCHEMISTRy

diketomaleie aeid + HzOz

disulfide bond

NAD(P)

DL-3,5/4,6-tetrahydroxyeyclohexane1,2-dione

benzaldehyde + forroie aeid

unknown

3,4',7-trihydroxyflavanone + 4',6dihydroxy-2-(a.hydroxybenzyl) eoumaranone

benzoxepinone-spiro eyclohexadienone

4',7-dihydroxyflavon-3-o1

Chance (1952)

973

Akazawa and Conn (1958)

681a

350

618

1076

1149

996

24

Decarboxylation

oxaloacetate (Mn2+)

syringic acid

vanillic acid

Halogenation

tyrosine + r(or 1 )

2

Hydroxylations

p-hydroxyphenylacetonitrile (Mn2+)

tyrosine

tyrosine (DHF)


malonate Shannon, de VeiHis and Lew (1963)

2,6-dimethoxy-p 97,703 benzoquinone

4,4'-dimethoxy-2,5, 97 2'5'-dibenzoquinone

methoxy-p-benzoquinone 703

3-monoiodotyrosine 85

p-hydroxymandelonitrile 765

dihydroxyphenylalanine 997

dihydroxyphenylalanine Buhler and Mason (1961)

Polymerization (condensation)

phenol 0,0'-biphenol 273

tyrosine dimer (0,0' -biphenyl linkage)

lignins

83

25 BIOCHEMISTRY

2.3.2. IAA degradation

Evidence has accumulated which indicates that the reaction of HRP with IAA differs from those with other substrates such as NADH and DHF. It is indeed very interesting to note here a feature of IAAHRP reactions that is rather similar to an oxygenase type. Through the efforts of many workers (Kenten, 1955; Ray, 1956; Ray and Thimann, 1956; Morita et al., 1962; 1967; Hinman and Lang, 1965) the following stoichiometry has been confirmed :

~CH2COOH

~ .. ) + °2N

H lperoxidase

~CHO ~CH2 ~J or ~",A

° +C02 +H2 0

H ~

The products were found to be indole-3-aldehyde and 3-methylene oxindole. Morita et al. (1962) showed that the dominant product was indole-3-aldehyde when higher enzyme concentrations were used. Apparently the reaction is similar to the lactate oxidative decarboxylase reaction, which is monooxygenase type (Bloch and Hayaishi, 1966) or an internai mixed function oxidase type (Mason, 1965). Indole-3-acetic acid was found to react with HRP Compound III at a relatively high rate (Yamazaki et al., 1965; Yokota and Yamazaki, 1965; 1312). In this respect the reaction is similar 10 the tryptophan pyrrolase reaction, in which the oxygenated enzyme was considered to be an obligatory intermediate (Ishimura et al., 1967; 605a). Many features of the mechanism of the IAA reaction, however, still remain to be elucidated. The key points of the mechanism can be summarized as follows :


a. The IAA free radical formed by peroxidase catalysis is an important intermediate (Hinman and Lang, 1965; Morita et al., 1967; Yamazaki and Souzu, 1960; Ray, 1960, 1962; Ricard and Nari, 1966, 1967; 924). Hinman and Lang (1965) proposed a mechanism in which the radical reacts with molecular oxygen to fonn 3-methylene oxindole as a main product through several nonenzymic steps (Fig. 6a). Although it is unknown whether the radical is free or attached to the enzyme, it may react with external oxidants such as ferric cytochrome c and ferric o-phenanthroline complexes (Yamazaki and Souzu, 1960). A question which arises is why the nature of the final products depends upon the concentration of enzymes in the reaction (Morita et al., 1962, 1967; Hinman and Lang, 1965). An answer to this question is proposed through the reaction scheme (Fig. 6b) of Bemiller and Colilla (90). The proposed pathway requires as a key step a two-electron oxidation catalyzed by a metal ion, be it the iron of the peroxidase heme or Mn3

+. It is proposed that the enzyme oxidizes Mn2

+ to Mn3 + and that IAA is subsequently

oxidized non-enzymatically by Mn3 + to 3-methylene-indolenine with

the kind and amount of subsequent products being detennined by the pH and composition of the reaction mixture. This scheme also explains the ability of cx-methyl-IAA and cx,cx-dimethyl-IAA to act as substrates for peroxidases, while indole-3-propionic and indole3-butyric acids cannat.

b. During the reaction with IAA a part of the enzyme, spectrally similar ta Compounds II and III is observed as an intennediate (Morita et al., 1967; Yamazaki and Souzu, 1960; Ricard and Nari, 1966, 1967; Fox et al., 1965; Degn, 1969; 697, 875). From the visible spectrum between 500 and 600 nm the intennediate is judged to be Compound III at around pH 4.0 (Morita et al., 1967) and Compound II at pH 5.0 (Fox et al., 1965; 1461). It has been concluded that Compound III, accumulated during the reactions of DHF and NADH, is not a Michaelis type of intennediate (Chance, 1952; Yokota and Yamazaki, 1965; Yamazaki and Piette, 1963). Since IAA .!eacts ~R~!!?-p~~~~.~~~.at a.~~~E~~J!.LJJigh !2te, ~tion of~~ml?2...l!.~~L!!L9Ùr..mK.Jhe.JAA.....Q!-~<!~tion must have a positIve mèaniQKin the catalysis. However, it is still uncertam whetIféfôTnotth~ mai~rëactron' proceeds via Compound II or III, mainly because of the difficulty in distinguishing between these two HRP compounds.

"(06) 1l1l!10.) pUll J;JII!W;J8 J;J!JV "q "(Zn7 oS11l ;J;Js) Ç961 'l}ul11 pUll UIlWU!H J;J!JV "11

·UO!lllpI1Jl};Jp VV( JOj SlillM41lld p;JsodoJd

c

-~ -~ :I:% I%9 o %8.~4o 0-0-08 40 8l 1 N o n n/ ni

IO<9 ~ @ J' © N n

l

8o o-~ l

I%

Ô N~ 8 l

A1I1.SIW3H:J0I8


c. A small amount of HzOz eliminates the lag phase and promotes the 0z-consuming oxidation of IAA under certain experimental conditions (Kenten, 1955; Yamazaki and Souzu, 1960; Ray, 1960, 1962; Shin and Nakamura, 1962; Morita et al., 1967). It is also true that the inhibition by catalase is negligible under certain experimental conditions (Fox et al., 1965; 1461). Consequently, the raie of HzOz does not appear to be essential even as an initiator of the reaction. Using superoxide dismutase, it has recently been found that superoxide anions are not involved in the reactions of IAA with HRP (875, 1461). This fact seems to be a peculiar property of the IAA reaction since the oxidations of NADH and DHF by HRP are strongly inhibited by superoxide dismutase (1461). This fact is compatible with the mechanism (Hinman and Lang, 1965; Ray, 1962) that the IAA peroxide radical instead of the superoxide anion radical is a product of the reaction between the IAA radical and Oz (see also 697). A significant question to be answered is how the IAA radical can be formed without an involvement of the superoxide anions. An answer to this question is given by Ricard and Nari. The mechanism they praposed (852; Nari, 1967; Nari et al., 1967; Ricard and Nari, 1966; Ricard and Nari, 1967; Ricard, 1969) involves the effective participation of ferroperoxidase in IAA oxidation (already postulated by Ray, 1960), at acidic pH and is based on the following arguments :

1) Carboxyferroperoxidase is partially decomposed by light (Iight suppresses the CO inhibition of IAA-oxidase) not into ferro- but into ferriperoxidase. CO inhibition and its suppression by light argue against the participation of a unique free radicals'chain. Thus contrary to Yamazaki's opinion, peroxidase reduction cannot be entirely due to highly reducing radicals generated through prior formation of Compounds 1 and II. Furthermore peroxidase reduction is obtained in a medium in such poor oxygen content that IAA destruction does not occur and evidently in these conditions, IAA autooxidation cannot occur and consequently no peroxide can be formed.

2) Substances such as IBA (indolebutyric acid), IPA (indolepropionic acid) which appear unable to reduce peroxide (and indicators such as methylene blue, Laught violet and phenosafranin which are reduced by IAA) are not degradable in the absence of peroxide.

29 BIOCHEMISTRy

3) The impossibility of a complete inhibition of IAA degradation by high catalase concentrations (Iargely sufficient to completely inhibit the typical peroxidation of IBA and IPA) which cannot be interpreted otherwise than by a partial IAA oxidation without a peroxide requirement.

4) Cyanide does not stop the reaction when added during its course. When present in the mixture before the reaction initiation, the reaction is completely blocked even in presence of H 0 •

2 2

Ricard's group furthermore demonstrated that Compound III (obtained by reduction of ferriperoxidase in the presence of methylviologen and 0) is decomposed by IAA which is simultaneously destroyed. This was confirmed by Yamazaki et al. (1967). Indoleacrylic

•acid is similarly destroyed by Compound III (429).

Klapper and Hackett's proposaIs and partiaily those of Yamazaki's group were integrated in a summary scheme (Fig. 7a) by Ricard and Nari (1966).

This scheme shows that IAA can be destroyed in the absence of peroxide :

a) either through a typical peroxidase reaction (peroxide is formed in the mixture) involving Fe 3+, C l, C II and free radicals of IAA,

p

b) or through a cycle involving Fe 2+ and C III. p

The latter functions only at acidic pHs (3 to 4), is blocked by carbon monoxide (to form carboxyferroperoxidase) and by ferricyanide (which oxidizes Fe 2+ into Fe 3+) as weil. The former peroxidase reaction is insensitive to these two s~bstances. The whole system is dependent upon the IAA-mediated ferriperoxidase reduction into ferroperoxidase.

Employing stopped-flow and low-temperature spectroscopic techniques, Ricard and Job (110 1) further elucidated the reaction sequences and the nature of the intermediate peroxidase compounds leading either to indole-3-aldehyde or to methyleneoxindole (Fig. 7b).


COMPfUNO Il

o COMPOUND 1 [:0.

~--....,..,H202 ----.f -=--~-"'.Fe 3+

IAA f ~F~ ox

---- COMPOUND 1I1..Jl--IAA

(FepO~+)®r Fe~+~IAA

P2 !_ IAA peroxide.LIAÂ- FeJ+ IAA

3-methyleneoxindole j;s: : 2+

COMPOUND 1 !'d Fep +~----.,IAA;:::::::,. epoxIe + lAI>: COMPOUNUDI COMPOUND III

1AAi Jt Fe 3+IAA· Fe 3+0'

IAA-? 2p r Oz 3+· F':+3+0.- Fe 2+IAAO-Fep IAA02 CO2 ep 2 IAA P 2

l:AA ~C02+0W 21 A A' 4 \ Fe~+02'-IAA2 FeJ+epoxide

indole-3 -aldehyde

u O2 CO2

1AA' ---":::::""'IAAOi ~epoxide ..{>3-methyleneoxindole

Fig. 7. a. Possible pathways for IAA degradation by HRP(afier Ricard and Nan, 1966).

b. 1. Proposed reaction sequences for the oxygen consuming degradation of IAA.

II. Non-enzymatic evolution of IAA free radical to methylene oxindole (afier Ricard and lob, 110 1).

BIOCHEMISTRY 31

It can be added that the ferric enzyme could be reduced by the IAA free radical rather than by IAA itself (924). In addition to these pathways, it must be mentioned that a considerable amount ofperoxidase is inactivated during the oxidation of IAA (Fox et al., 1965). The process of heme degradation has been described by Yamazaki (1459).

Isoenzymes involved in IAA destruction

To date, three hypotheses, with varying degrees of substantiating evidence, have been suggested in relation to the molecular 'residence' (582) of IAA oxidase activity. The first considers that the two types of activity (i.e., IAA oxidase and peroxidase) are present on separable and distinct enzymes; the second considers that the two types of activity are resident on one enzyme (peroxidase) but with two active centers; and the third calls attention to the presence of peroxidase isoenzymes where one member of the family of isoenzymes may be the primary residence of IAA activity. These alternatives are examined briefly.

The idea of separate enzymes was reported by Sequeira and Mineo (1966). They had noted that fresh preparations (tobacco roots) lost IAA oxidase activity after several weeks in storage, whereas peroxidase activity was unchanged. Further, they found that thermal inactivation points and pH optima were different. Attempts to separate the two types of activity on columns of silica gel, carboxymethyl cellulose, diethylaminoethyl cellulose, and diethylaminonethyl Sephadex failed, but with SE-Sephadex and 0.1 M eluting buffer they reported a major IAA oxidase peak (at 5.4 elution volumes) with little or no peroxidase activity from both tobacco root extracts and commercial HRP. Hoyle results (582) obtained with the same HRP and a purified Betula enzyme preparation did not support Sequeira and Mineo's contention.

The belief that both types of activity reside in one enzyme (i.e., peroxidase) is more widely held. Evidence offered in support of this belief is mainly that both types of enzyme activity remain together through various stages of purification and also there is evidence that thermal inactivation is the same for both (Ray, 1960). The work of Siegel and Galston (1967, confirmed by Hoyle, 582) suggests that the dual catalytic functions of peroxidase may result from two active sites on the enzyme. By separating the apoenzyme from its heme prosthetic group with acidified acetone, they found that apoenzyme alone would


oxidize IAA, but was devoid of peroxidase activity. However, partial restoration of peroxidase activity occurred with recombination of heme and apoenzyme. They concluded that apoenzyme possesses the IAA oxidase function, and that a heme-protein attachment is needed for the peroxidase function.

Their work was challenged by Ku et al. (709) who used a mixture of an acid and butanone (instead of the acid-acetone) for dissociation of the heme group from its apoenzyme and were not able to effect the oxidation of IAA in the presence of the apoenzyme alone or with Mn2

+ and DCP as cofactors. The residual enzyme activity of the apoenzyme thus might be due to a slight contamination by unresolved holoenzyme in that fraction rather than to the apoenzyme itself.

In most studies, the total oxidase and/or peroxidase activity has been measured without consideration of the multiple forros of an enzyme (i.e. isoenzymes). MacNicol (1966) has separated four isoenzymes (three cationic and one neutral) from Alaska peas. He found that aIl of the isoenzymes could catalyze the peroxidation of guaiacol and the oxidation of IAA, but the C cationic species had an IAA oxidase

J guaiacol peroxidase ratio that was 10-fold higher than the next most active species.

There is probably no example in the literature of a peroxidase extract or purified isoperoxidase unable to develop a so-called IAAoxidase activity in vitro when placed in suitable conditions of pH and effectors, and/or after adequate purification (473). The question thus is whether any peroxidase isoenzyme encounters such favourable conditions - and IAA - in situ in order to develop the auxinolytic activity.

IAA destruction capacity of different types of isoperoxidases has been studied in vitro (697, 852, 1101). Mazza et al. (852) and Ricard et al. (1102) established a strong positive correlation between the oxygenase IAA-destroying activity (in absence of exogenously supplied peroxide or other cofactors) of different purified turnip peroxidases and their midpoint oxido-reduction potential value. They concluded that the most basic isoenzyme was the best candidate to be 'IAA-oxidase' in vivo. Nakajima and Yamazaki (924) showed that the oxygen-consuming oxidation of IAA occurred much faster in the presence of the HRP neutral isoenzyme C than in the presence of the acidic isoenzyme A. Physiological studies, which attempt to establish a relationship between endogenous IAA level, intensity of the IAA-dependent process and prior qualitative changes in peroxidase zymograms generally support the view that auxin catabolism is mediated by the most cationic isozymes (see Section 5.1).

BIOCHEMISTRy 33

The oxidation of IAA by a purified anionic tomato peroxidase (697) was found to be negligible unless reaction mixtures were supplemented with H

20

2• A similar dependence on H

20

2 has been

shown for the IAA oxidase-peroxidase complex of yellow birch (587). From a physiological standpoint, such a result suggests that the destruction of IAA in tissue could be controlled by the availability of H

20

2 or other peroxides, as probably are lignin and ethylene biosynthesis.

This view was first expressed by Siegel and Galston (1955) and has been extended to coyer the role of auxin protectors (1281).

2.3.3. H 0 formation and lignin biosynthesis 2 2

Metabolic pathways leading to the main families of plant phenolic compounds are relatively weil known. Shikimic acid and cinnamic acid pathways constitute a common sequence from which originate the different groups of polyphenols and lignin particularly (Fig. 8).

The pathway of lignin biosynthesis and the enzymes involved are weil established. Several excellent recent reviews treat these subjects in detail (20,890a). Phenylalanine ammonia Iyase (PAL) catalyzes the conversion of phenylalanine to trans-cinnamic acid. Cinnamic acid is hydroxylated at the para position by cinnamic acid-4-hydroxylase to form p-coumaric acid; however, p-coumaric may also be formed by the deamination of tyrosine catalyzed by tyrosine ammonia Iyase. pCoumaric acid is further hydroxylated by p-coumaric acid hydroxylase to give caffeic acid. o-Methyltransferase then methylates caffeic acid to ferulic acid. Sinapic acid is formed by hydroxylation and methylation of ferulic acid. Coumaric, ferulic, and sinapic acid are converted to their respective CoA esters by cinnamate acid-CoA-ligase. The esters of cinnamic acid derivatives are reduced to the corresponding aldehydes and further reduced to alcohols by cinnamoyl-CoA-oxidoreductase and cinnamyl alcohol dehydrogenase. These enzymes would form the cinnamylic alcohols into the secretory vesicles during their migration towards the wall.


phenylalanine

~ cinnamic acid caffeic acid

~ ft ~ ~ p-co~oriC ocid~ferUI~oCid%,OPiC acid

CinnO~YI CoA esters tyrosine

cinnamyl aldehydes

cr lignins 4@1--- cinnamyl alcohols

Fig. 8. Metabolic pathway and enzymes involved in lignin biosynthesis: l. phenylalanine ammonia Iyase 2. cinnamic acid-4-hydroxylase 3. p-coumaric hydroxylase 4. o-methyltransferase 5. cinnamic acid-CoAligase 6. cinnamoyl-CoA-oxidoreductase 7. cinnamyl alcohol dehydrogenase 8. peroxidases.

Polymerization due to peroxidase could begin during this transport (20). Polycondensation of the cinnamyl alcohols probably occurs through the mediation of wall peroxidases. Free radicals, formed by oxidation of these alcohols by peroxidase-H

20

2 exist in several resonance forms

and couple in an essentially random manner, although participation of the more stable resonance forms is statistically favored. Coupling between radicals of the alcohols occurs readily. In the lignifying plant cell wall, however, coupling is primarily between incoming radical species and the growing lignin polymer which itself contains phenolic hydroxyl groups that are oxidized to radicals by peroxidase.

BIOCHEMISTRY 35

Since different esters of cinnamic acids have been identified in sorne lignins, it is conceivable that sorne vesicles, unfused and lacking reductases, directly bring their esters to the wall, where further transesterification occurs.

A review of the available data on the localization in the cell of the enzymes of phenolic metabolisrn, the organization of the different sequences at the subcellular level, the existence of transport processes between different organelles and finally the participation of soluble and wall-peroxidases in lignin formation and integration in the wall has been presented schematically (Fig. 9) by Alibert et al. (20),

pheny 1- alanine

----------t------------------ENDOPL ASMIC

RETICULUM --------i-----i-------------j---GOLGI cinnamic A PPARATUS caffeic acids

'dp - cou!.ma ri c .derP 0 x 1 ose s . . oc 1 s

SECRETORY VESICLES

Slna!1C

p-coumarate-CoA sinapate-CoA

cinntmYliC alcohols

dimerization .. _ poly mer iz a tian

ci nnom y 1ici i 9 n i ilS '1i-- - - - - - - - - - - - - - Pe r 0 x id ose s esters -----___.WALL bound to li gn ins - - - - - - -H20 2

Fig 9. Fonnation of lignin precursors and lignin in the cell (after Alibert el al.. 20),

36 PEROXIDASES 197011980

Peroxidase involvement

On the basis of histochemical studies, Freudenberg et al. (1952) proposed that peroxidase was involved in lignification in vivo in spruce. This view was supported by the work of Jensen (1955), and Siegel (1956, 1957) who later demonstrated that peroxidase would efTect an in vitro oxidation of eugenol to a lignin-like substance. Later studies by Van Fleet (1959), Wardrop and Bland (1959), and Koblitz and Koblitz (1966) argued against the direct involvement of peroxidase in the lignification process. In particular these workers have shown that maximum peroxidase activity occurs in prolignifying tissues, and that activity declines after lignification of the primary wall has commenced. Further, De Jong (1967) daims never to have observed a positive peroxidase reaction in xylem.

The discrepancies might come from the fact that sorne observations concemed ail the year xylem without distinguishing the difTerentiating stages. A more recent study by Czaninski (264) indeed showed that during the difTerentiation of wheat vascular cells, longitudinal primary walls exhibit a strong peroxidase activity. A similar reaction can be visualized in transverse walls but in this case, the contrast decreases sharply at the beginning of secondary wall deposition.

It is evident from studies such as those of Lipetz and Garro (1965) and Parish and Miller (1969), that there may be sorne relationship, even though an indirect one, between peroxidase and lignification. These workers have shown that treatments which cause leaching of wall-bound peroxidases also reduce lignification.

Isolated cell wal1s from Pinus ellioUii tissue cultures produce lignin having physical and chemical properties similar to that prepared from wood, when incubated in the presence of coniferyl alcohol and HzOz. The enzyme responsible for this production was shown to be peroxidase (1 436a). Indeed, 'laboratory' lignin can be prepared by the carefully controlled addition of dilute solutions of peroxidase and HzOz to a stirred solution of an appropriate mixture ofcinnamyl alcohols (Geissman and Grout, )969). However, it seems evident that only sorne of the various isoperoxidases isolated from plants are able to catalyze these reactions.

37 BIOCHEMISTRY

One may consider that peroxidases play a key role in the overall process of lignin formation by

1. generating HzOz necessary for oxidation and polymerization of cinnamyl alcohols (357, 488, 489, 808).

2. oxidizing cinnamyl alcohols to phenoxy radicals (525) with the rapid formation of oligomers.

3. converting ferulic to diferulic acid, which can act as a hemicellulose cross link (828a).

4. a) binding cinnamic acid to wall proteins or carbohydrates (1435, 1436, 1436a)

b) polymerizing cinnamyl alcohols in walls (Brown, 1961).

Formation of H2 0

Z by cel! walls and cinnamyl alcohols oxidation

Several factors appear to be of importance in the formation of HzO by cell walls with respect to the lignification process (357, 488, z 488a, 489, 518) :

1) A bound peroxidase catalyzes the formation of HzO at the expense z of NAD(P)H in a reaction that is stimulated by monophenols and Mnz

+. Similar reactions have also been reported for soluble peroxidases (Akazawa and Conn, 1958; 647).

2) HzO formation involves the superoxide radical 0z- as anz intermediate of the above-mentioned system.

3) 0z- equilibrates in part with a second mechanism, again producing HzO in a separate and peroxidase-independent system. z

4) The electron donor NADH can be provided by a bound malate dehydrogenase. In analogy to the known malate-oxalacetate shuttles, the possibility of a similar mechanism across the plasmalemma has


been discussed (488). By this means, cytoplasmic reducing equivalents could be provided to the cell wall. Furthermore, the concomitant removal of accumulating oxalacetate would positively affect the unfavorable equilibrium. of this reaction. Eventually, malate dehydrogenase is also part ~ enzyme-NADH complex susceptible to the attack of 0z- as discussed in the preceding Section.

The reactions outlined above are illustrated in Figure 10.

R'OH R'O·....lignin

HO ~H+ ._.' 2 2 ----0

02~ pe'M~\;~:~:~· 2

ROH -"RO' Y2

~NAD'~NADH~ ~NAD+

_ r i ~

malate dehydrogenase

WALL oxalo- ma/ate

acetate t-CYTOPLASM t

Fig. 10. Reactions generating hydrogen peroxide in higher plant cell wall (after Gross el al., 489).

Stimulation of H20

Z production by monophenols (and coniferyl

alcohol) is apparently due to their inhibiting effect on the formation of peroxidase Compound III (518) which appears as a blocker of HPz formation. It can also be mentioned here that the myeloperoxidase mediated H

Z0

2 formation accompanying phagocytosis also was related

to its NADPH oxidase activity in leukocytes (998a, 1308). Similarly the bactericidal activity of eosinophil peroxidase is seen through a perturbation of the plasma membrane with a respiratory burst, in which oxygen is converted to hydrogen peroxide (634, 635).

BIOCHEMISTRY 39

In comparison to previous theories on the origin of HzOz in cell waIls, the scheme proposed here offers several advantages. For example, the problems relatedto the transport of 'toxic' HzOz from cytoplasmatic sources to the cell wall compartment would be eliminated. Further, regulation of the lignification process would be facilitated, either by producing HzOz only within the lignifying areas or by degrading HzOz in the non lignifying parts by a wall-associated catalase that has been found in cell wall preparations (357). One also might visualize that both ROH and R'OH in Figure 10 represent hydroxycinnamyl alcohols. In this case, the operation of the entire reaction sequence would depend largely on the availability of these lignin precursors. The aforementioned appreciable stimulation of HzOz formation by coniferyl alcohol would support this idea. In this context, it should be noted that it was possible to polymerize coniferyl alcohol in vitro with this rather cornpIex system. Moreover, an analogous formation of HzOz has been reported with cell walls isolated from Forsythia xylem (448a). This result obtained with an actively lignifying tissue lends further support to the conclusions drawn above.

Three peroxidase isoenzyme groups found in cell walls of tobacco were tested for their capacity to form Hz Oz (808). Isoenzyme-group GI, located only in cell walls (GU and GIll are also found in protoplasts) showed the highest Kapp-value for HzOz formation. The lowest Kappvalue, i.e. maximal HzOz-formation, was received for group GIll which is ionically bound to cell wall. Stimulation of HzOz formation by coniferyl alcohol was much more significant than by p-coumaryl and sinapyl alcohol.

Gross' work (489) has been confirmed. Working with carnation stems, Czaninski and Catesson (191) discovered a heavy reaction in sieve plates after incubation in a medium containing DAB, malate, NAD and cofactors (MnClz and p-coumaric acid) as weil as in a medium containing only DAB and cofactors, i.e., in absence of exogenous HzOz. The fact that endogenous H 0 may be locally produced to start

2 Z the reaction is suggested by inhibition by catalase. On the other hand, phloem cell wall peroxidases were found to have no affinity towards cinnamic substrates except in differentiating and lignifying fibers. FinaIly, peroxidases reacting with syringaldazine can be localized in lignifying walls only (192).

::;.


Ferulic ta diferulic acids. Binding ta wall carbahydrate and pratein

Diferulic acid, bound by ester linkages, has been identified in smal1 amounts in water-insoluble pentosans (arabinoxylans) of wheat endosperm (828a) and in cell walls of Lalium (Hartley and Jones, 1976). Ferulic acid and diferulic acid are found in the ratio of 5: 1. The coupling of ferulic acid side groups, attached to arabinoxylan chains occurs through an oxidative phenolic coupling in which peroxidase is involved as il1ustrated in the following scheme (828a)

° -o-oMe M-o-eo 0 Arabino- Il Il r i -O-C-CH=CH If ~ OH + HO r; ~ CH=CH-C-o-{A abno xy1an } _ _ xylan

l Peroxidase H2 °2

MeC

If ~ CH=CH-~ ~ 0_[ Arabino-H xylan

Arabino- - J OH}-ol~-cH=cH xylan ~ JI ~

OMe

Whitmore (1435) examined the capacity of soluble, ionical1y- and covalently- bound peroxidase of slash pine callus and seedlings to catalyze the binding of ferulic acid to cell wall carbohydrates. By using caHus (which forms little lignin) and cambium cells from seedlings he was able to show that the wall-bound peroxidases, particularly the ionically-bound enzyme, catalyzed the coupling of ferulic acid to carbohydrate most efficiently. With cambial cells phenol-phenol bindings (as would be important in lignification) also occurred. In the same way wall peroxidases catalyze the incorporation of dehydrogenation polymer of coniferyl alcohol to wall protein containing hydroxyproline during the early stages of lignification (1436, 1436a).

41 BIOCHEMISTRY

Polymerization

The studies begun nearly four decades aga by Freudenberg in Germany have given us a much clearer idea of the nature of the polymerization processes which constitute lignification in the truest sense of the term. Freudenberg and Richtzenhain (1943) found that press juice .from a cornmon mushroom, Psalliota campestris, contained an enzyme system which could polymerize added coniferyl alcohol to an amorphous product bearing a striking resemblance in both chemical and physical properties to the natural lignin of conifers. It has since been established that the enzyme responsible for this polymerization is a phenol oxidase, laccase (Lyr, 1957; Freundenberg et al., 1958; Higuchi, 1958), but it was still not completely clear at that time whether the polymerization in higher plants was catalyzed chiefly by laccase or by peroxidase (Lyr, 1957; Higuchi and Ito, 1958). A freeradical mechanism has been proposed (see Brown, 1961) for the formation of these condensation products, in which the central intermediate in the formation of coniferyl-type polymers is a quinone methide, illustrated below :

00= CH-~H-CH20H H3CO

Sorne evidence for the existence of such an intermediate has been presented (Freudenberg et al., 1958). In a similar way the formation of a quinone methide from the dimer could lead to molecules with a higher degree of polymerization (Brown, 1961).

The three tobacco cell wall peroxidase isoenzyme-groups tested before (808) for their capacity to form H

20

2 (and phenoxy radicals of

cinnamyl alcohols, see above) were also tested for their polymerization capacity (807,808). Isoenzyme-group G l, located only in cell walls, yield maximal polymerization rates for coniferyl and p-coumaryl alcohol. G III (also found, in protoplasts) showed the lowest rates. The values obtained for H20 2 formation were opposite, thus pointing to possible


different catalytic functions of the peroxidase isoenzyme-groups within the œil wall. As a result, Miider et al. (808) proposed a scheme of lignification based on the different catalytic capacity of these peroxidase isoenzyme groups (Fig. 11).

malate malate dehyd ragenase

oxalaacetate

Fig. II. Involvement of three different groups of wall peroxidases (G!, II and III) in the lignification process (according to Miider et al., 808). .

OH R

RO«#O~B OH RO~Of B OH H0'Çr0§-0~R 1 1 - 1 - "'" 1 1 ~ OH

~:>.... OH C"'" OH H2 0 2 OR 0 OR 0 HO 8

Flayonol Choleon.

lpOO

H0'OQ=0 _ ,-dOH-0-~

:>.... 1 CH~OH H02C f B OH ~~ H02C) \;;d

o Auronr a.nzoit acid Cinnamic acid

~/H202 iPOO/H2 0 2~A+Pt-

~ Q HO~OOHH0'Çr:0H HOÇQO ?'B~H02 C ~OCH3 1 1 1 + 1 1 POO 1 - R "'" OH:::"" 4:-:-=--"'" H

R 2 H20 2 H o OH OH 0 OH 0

Flavanon.

Fig. 12. Involvement of peroxidases (POO) in catabolic pathways of fJavonoids in plant cell cultures (after Barz and Nicolas, 1978).

H20 2

lignins

Phenolics and extensin

BIOCHEMISTRY 43

No direct evidence is available to indicate that phenolics are indeed cross-linked to extensin, although phenolics do occur in smaIl amounts in cell walls. In this respect the catabolism of phenolics is often overlooked. Barz and Nicolas (1978) indicated that peroxidases play a very important role in oxidizing various flavonoids and aromatic acids (Fig. 12). Zaprometov (1978) has also indicated that the lactonization step in coumarin biosynthesis may take place with the formation of free radicals generated through peroxidase. Many of these phenolics are found in cell walls.

FinaIly, it is not clear whether the carbohydrate present in peroxidase is there as a functional prosthetic group - in which case peroxidase would have two prosthetic groups - or if the carbohydrate which was added to the synthesized polypeptide, is simply there for transportation out of the cell to become incorporated into the hemicellulosic fraction of the cell wall, in the synthesis of which peroxidase plays a role.

Lignin degradation

Lignin degradation, namely by microorganisms, has been long suspected to involve polyphenoloxidases such as peroxidase and laccase. Based on multiple observations, a growing concept is being developed that freely soluble peroxidase is not a lignolytic enzyme (529).


2.3.4. Ethylene biosynthesis

The fonnation of ethy1ene during the degradation or peroxidation of many kinds of organic mo1ecu1es has 1ed to extended studies of nonenzymic systems and the consideration that sorne of these mode1 systems might be operative in vivo (Osborne, 1978; 763a). Cu ions in particu1ar induce a 1ight-driven peroxidation of membrane 1ipids 1eading to ethy1ene fonnation (Sandmann and Bogger, 1980). As far as the enzymatic synthesis of ethy1ene is concerned, on1y one substance is known with certainty to be a precursor in vivo : L-methionine. Methionine is converted enzymatically (by a transaminase) to cx-hydroxyy-methy1thiobutyric acid and further to cx-keto-y-methylthiobutyric acid (KMBA) and non-enzymatically (through the 1ight mediated action of flavine mononucleotide FMN) to methiona1 (Bmethy1thiopropiona1dehyde). In a further in vitro but enzymic system consisting of precursor + peroxidase + cofactors, Ku et al. (1967, 1969) found that both methiona1 and KMBA 1ed to ethy1ene fonnation (Fig. 13). Ana1yzing their enzymic system, Mapson and Warda1e (1968) observed that next to peroxidase, a glucose-oxidase (generating peroxide) and two cofactors, an ester of p-coumaric acid and methanesu1phinic acid (Mapson and Mead, 1968; Mapson et al., 1969) were necessary for the conversion of a cx-hydroxy-y-methy1thiobutyric acid or KMBA to ethy1ene. These two latter substances, as weIl as methiona1, however were inactive in (non-buffer) intracellu1ar conversion systems.

Yang (1968) also showed that ethylene is rapidly fonned from methional or from KMBA by HRP in the presence of Mnz+, sot, oxygen and a specific phenol (the active phenols include sorne monophenols and rn-diphenols).

These two non-enzymic and peroxidase mediated ethylene generation schemes present sorne similarities with the two possible mechanisms of ethylene generation during host defense by neutrophils (neutrophil is one of five types of leukocytes which circulate in the blood and function as key elements in the defense of the host against invading pathogenic organisms) (Tauber and Babior, 1977, 1978; Weiss et al., 1977). The best characterized oxygen-requiring bactericidal mechanism in neutrophils is the myeloperoxidase-dependent system, in which myeloperoxidase mediates bacterial killing in the presence of HzO andz

45 BIOCHEMISTRY

CH,-5-CH2 - CH2- CH (NH2 l-COOH 1

(methionine)

.t CH 3-S-CH2-CH 2 -CH (OH )-COOH

(O(. - hydroxy- K- methylthiobutyrie aeid)

~ CH3-S-C H2 - C H2 -CO- COOH CH3 -S-CH2- CH2- CHa

(0(- keto-~- methylthiobutyrie aeid, KMBA) (methional)

0(.- D- glucose + glucose oxidase ....H2 ~

(H2 0 2 ) + peroxidase

{

P- cournarie ester

+ 1+ eofadors

methanesulphinie aeid

CH2 = CH2

\0 :r

o "'

(ethylene)

+ CH 3 -S-S-CH 3

(methyl disul fide )

+ HCOOH

(formie acid)

Fig 13. Alternative pathways of ethylene biosynthesis from methionine.


a halide ion (probably Cl~ in the intact neutrophil). The H,O, used by this system arises by the dismutation of 0,-, the product -of an enzyme-catalyzed reaction in which NADPH reduces oxygen by one electron. The O,--forming system is dormant in resting cells, but is activated on exposure of the ceIls to suitable stimuli; the changes in oxygen metabolism that result from the activation of this system are designated the 'respiratory burst'. It was later shown that stimulated neutrophils produce the highly reactive oxidizing hydroxyl radical OH", which releases ethylene from methional (scheme beJow), and that the O - generated during the respiratory burst is involved in the production

2 of this reactive species :

H 0 + O - ~ OH" + OH- + O22 2 2

CH S - CH2 - CH2 - CHO + OH"--. CH S+ - CH - CHO + OH3 3 2

CH $'" - CH - CH - CHO + OH~ 1/2 (CH S)2+ HCOOH + CH = CH23 2 2 3 2

The production of ethylene from methionine by Fentom's reagent (Fe-++ plus H,O,), a weil characterized source of OH", lends further support to the cliim that methional is oxidized to ethylene by OH".

Two purified horseradish isozymes differing in their specific peroxidase activity were tested as to their ethylene formation capacity (Yang, 1968). Although the anionic A-I isozyme had higher specific peroxidase activity (as measured by the peroxidation of o-dianisidine) than the cationic C isozyme, C isozyme was about 250 times more active (per unit peroxidase activity) than isozyme A-I in catalyzing ethylene formation from methional. More recent labeling studies of Adams and Yang (1979) provided evidence that ethylene was synthesized in apple tissue from methionine via S-adenosyl-methionine (SAM, after activation of methionine by ATP as the first reaction) and a 4-carbon amino acid, l-aminocyclopropane-1 carboxylic acid (ACe), i.e. : methionine ~SAM --.ACC ---+ethylene. The conversion of ACC to C

2H

4 was inhibited by anaerobic atmosphere, free radical scavengers

and strong reducing agents. The reaction converting ACC to C2H4

was

BIOCHEMISTRY 47

also inhibited strongly by various copper chelating agents (Apelbaum et al., 1981), which suggests that a copper enzyme, possibly a copperperoxidase, may be involved in the final step of C H biosynthesis.

2 4

The inhibitory phenomena are in accord with the known 02 requirements for C H production (Lieberman, 1979), which now can be related to

2 4 the final reaction step from ACC to C

2H

4•

ln vivo peroxidase involvement ?

It is however doubtful if peroxidase is involved in the intracellular conversion, for additions of catalase enhance, rather than reduce, ethylene production, and endogenous peroxidase activity does not parallel ethylene production (Kang et al., 1971).

The relationship of the peroxidative indoleacetic acid oxidase system to in vivo ethylene synthesis in cotton was examined by Fowler and Morgan (398). Modifications of peroxidase and IAA oxidase activity in auxin-treated plants occurred weil after the elevation of internai ethylene levels. This would indicate that the enzymes are not ratelimiting factors when ethylene synthesis is increased. It seems also unlikely that peroxidase plays a role in producing C H from methionine

2 4 in the mungbean hypocotyl because chlorogenic or cafTeic acid, potent inhibitors of peroxidase-catalyzed C H formation from methionine

2 4 analogs, did not inhibit C H production in this tissue even at 0.5

2 4 mM (Sakai and Imaseki, 1972). It can be argued that sorne isoperoxidases only are concerned with the process. Considerable evidence indeed now links the rates of ethylene production of growing or expanding tissues with their levels of endogenous auxin and applications of auxin to isolated plant parts invariably enhance the evolution of ethylene (Osborne, 1978; Dubucq el al., 1978; Hofinger el al., 1980).

Since the specific activity of ethylene produced from C4C) methionine was similar in control and auxin stimulated treatments, Sakai and Imaseki (1972) concluded that the efTect of auxin was to stimulate the enzyme system converting methionine to ethylene, and not to enhance the formation of methionine. In addition, the Steen and Chadwick (1973) proposai that auxin has two efTects on ethylene biosynthesis, one immediate and cycloheximide-insensitive stimulation and a second,


occurring after a lag period of 1-2 hr, which is sensItive to protein synthesis inhibitors, has some striking paralle1ism with simi1ar immediate and delayed auxin effects on activity and synthesis of specific peroxidases (Ga1ston et al., 1968).

ACC can be converted to C H in model systems which invo1ve 2 4

an oxidation reaction requiring H)O) (Bolier et al., 1979; Lizada and Yang, 1979). This suggests the possibi1ity of an in vivo peroxidase system, which cou1d react with ACC to form C

2H

4• Current1y, there

is no good evidence for such an in vivo reaction. However, the in vitro system iso1ated from pea seed1ings by Konze and Kende (697a) suggests such a system. Presumably, the enzyme could be present constitutive1y in all tissues. It may be membrane-associated, for it did not survive treatment with surface-active agents, and coId or osmotic shock reduced the capacity of the system to convert ACC to C H • Such treatments

2 4will affect peroxidase binding to membrane (see Chapter 3).

There is also some striking resemblance between the stimulated H)O)-dependent lignin synthesis and the increased ethylene synthesis düe -to the release and increased activity of the H

20

2 forming glucose

oxidase enzyme apparently attached to plant cell-wall material (and liberated by the action of bacterial pectic enzymes as an example, Lund and Mapson, 1970).

2.4. TYPES OF PEROXIDASES

Besides the higher plant peroxidases EC 1.11.1.7 which catalyze the reactions mentioned in section 2.3.1, peroxidases from other sources have been found with a particular affinity for specific substrates. Some of them received a different code number in the enzyme nomenclature. They are listed here below.

BfOCHEMfSTRY 49

Ascorbate peroxidase

L-ascorbic acid : hydrogen peroxide oxidoreductase Ascorbate + H 0 = dehydroascorbate + 2 H 0

2 2 2

Other donors : pyrogallol, guaiacol, 1-: Sources : higher plants, algae. References: 673, 1207.

Bromoperoxidase (Bromide peroxidase)

Bromide : hydrogen peroxide oxidoreductase p-hydroxybenzyl alcohol + Br-+ H,O, = 3-bromo-p-hydroxybenzyl alcohol Ferriprotoporphyrin IX, glycoprôteln. Other donors : 1-: / Sources : algae, marine invertebrates. References: 7, 50, 1009.

Ch/oride peroxidase (Ch/oroperoxidase)

Chloride : hydrogen peroxidase oxidoreductase. EC 1.11.1.10. 2 RH + 2 CI- + H,O, = 2 RCI + 2 H,O Ferriprotoporphyrin ïx, glycoprotein. -Other donors : I~ Br-: Sources : fungi. References: 246, 505,1325, Morris and Hager (1966).

Cytochrome C peroxidase

Ferrocytochrome c : hydrogen peroxide oxidoreductase. EC 1.11.1.5. Cytochrome c2

+ + H,O, = cytochrome c3 +

Ferriprotoporphyrin -IX. Sources : aerobically grown yeast. References: 170, 252, 328, 362, 363, 885, 941, 945, 1437.


lodide peroxidase (/odopemr:idase)

lodide : hydrogen peroxide oxidoreductase. EC 1.11.1.8. 1- + H,O, + tyrosine = iodotyrosine + 2 HoO 21-+H,O,=I,+2H,O Sources- : -thyroid, algù. References : 915, 922.

Glutathione peroxidase

Glutathione : hydrogen peroxide oxidoreductase. EC 1.11.1.9. Glutathione + ROOH = glutathione oxided Selenium containing. Sources : animaIs : mitochondria and cytoso!. References: 474, 516, 783.

Lactoperoxidase

Donor : hydrogen peroxide oxidoreductase. EC 1.11.1. 7. Its electron donor profile only difTers from that of plant peroxidases regarding halide ions. Derivative of mesoheme IX, glycoprotein. Sources : milk, saliva. References : 907, 1003, Hultquist and Morrison (1963).

Myeloperoxidase (Verdoperoxidase)

Donor : hydrogen peroxide oxidoreductase. EC 1.1 1.1.7. Its electron donor profile only difTers from that of plant peroxidases regarding halide ions. Sources : leukocytes, macrophages. References : 893, 965, 1123, 1308.

BIOCHEMISTRy 51

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NARI, J. 1967. Contribution à l'étude de quelques réactions d'oxydation catalysées par la peroxydase de Raifort. Thèse (No. enregistrement C.N.R.S. : 1632) Univ. Aix-Marseille.

NARI, J.; PENON, P. 1968. Nature des composés hématiniques chez les végétaux. PHYSIOL. VEG. 6: 47-66.

NARI, J.; RICARD, J.; VINCENT, M. 1967. Contribution à l'étude de la formation de divers composés de la peroxydase de Raifort en présence de l'acide ~-indolylacétique. C.R. ACAD. Sc. PARIS 264: 1108-1111.

OSBORNE, D.J. 1978. Ethylene. In 'PHYTOHORMONES AND RELATED COMPOUNDS - A COMPREHENSIVE TREATISE, VOL. l'. Letham, O.S.; Goodwin, P.B.; Higgins, T.J.V. (Eds). Elsevier - North-Holland Biomedical Press, pp. 265-294.

PARISH, R.W.; MILLER, F.L. 1969. The uptake and efTects of calcium and phosphate on maturity, lignification and peroxidase activityon wheat intemodes. AUST. J. BIOL. SCI. 22: 77-85.

57 BIOCHEMISTRY

PARUPS, E.V. 1969. Involvement of free radicals in the oxidative degradation of indole-3-acetic acid. CAN. J. BIOCHEM. 47: 220-224.

PAUL, K.G. 1958. Die Isolierung von Meerrettich-Peroxydase. ACTA CHEM. SCAND. 12: 1312-1318.

PIETTE, L.H.; YAMAZAKI, 1.; MASON, H.S. 1961. In 'FREE RADICALS IN BIOLOGICAL SYSTEMS'. Blois, M.S. et al. (Eds). Academie Press, New York, p. 195.

RAY, P.M. 1956. The destruction of indoJeacetic acid. II. Spectrophotometric study of the enzymatic reaction. ARCH. BIOCHEM. BIOPHYS. 64: 193-216.

RAY, P.M. 1960. The destruction of indoleacetic acid. III. Relationships between peroxidase action and indoleacetic acid oxidation. ARCH. BIOCHEM. BIOPHYS. 87: 19-30.

RAY, P.M. 1962. Destruction of indo1eacetic acid. IV. Kinetics ofenzymicoxidation. ARCH. BIOCHEM. BIOPHYS. 96: 199-209.

RAY, P.M.; THIMANN, K.V. 1956. The destruction of indole acetic acid. Action of the enzyme from Omphalia fla vida. ARCH. BIOCHEM. BIOPHYS. 64: 175-192.

RICARD, J.; NARI, J. 1966. Contribution à l'étude des mécanismes de la dégradation de l'acide ~-indolylacétique par la peroxydase de Raifort. BlOCHlM. BIOPHYS. ACTA 113: 57-70.

RICARD, J.; NARI, J. 1966. Mise en évidence de la réactivité de l'oxyferroperoxydase. c.R. ACAD. Sc. PARIS 262: 1784-1787.

RICARD, J.; NARI, J. 1966. Réduction de la peroxydase de Raifort par l'acide J3-indolylacétique. C.R. ACAD. Sc. PARIS 262: 1898-1900.

RICARD, J.; NARI, J. 1966. Les réactions d'oxygénation catalysées par la peroxydase. BULL. SOc. FRANC. PHYSIOL. VEG. 12: 29-43.

RICARD, J.; NARI, J. 1967. The formation and reactivity of peroxidase compound III. BIOCHIM. BIOPHYS. ACTA 132: 321-329.

RICARD, J. 1969. Les peroxydases des végétaux supérieurs. BULL. SOc. FRANC. PHYSIOL. VEG. 15: 331-362.

SAKAI, S.; IMASEKI, H. 1972. Ethylene biosynthesis: methionine as an in vivo precursor of ethylene in auxin-treated mungbean hypocotyl segments. PLANTA 105: 165-173.

SANDMANN, G.; BOEGER, P. 1980. Copper-mediated lipid peroxidation processes in photosynthetic membranes. PLANT PHYSIOL. 66: 797-800.


SEQUEIRA, L.; MINEO, L. 1966. Partial purification and kinetics of indoleacetic acid oxidase from tobacco roots. PLANT PHYSIOL. 41: 1200-1208.

SHANNON, L.M.; DE VELUS, J.; LEW, J.Y. 1963. Malonie acid biosynthesis in bush bean roots. II. Purification and properties of enzyme catalyzing oxidative decarboxylation of oxaloacetate. PLANT PHYSIOL. 38: 691-697.

SHANNON, L.M.; KAY, E.; LEW, J.Y. 1966. Peroxidase isozymes from horseradish roots. 1. Isolation and physical properties. J. BIOL. CHEM. 241: 2166-2172.

SHIM IZU, K.; MORITA, Y. 1966. Studies on phyto-peroxidase. XVIII. Chemical composition of japanese-radish peroxidase c. AGR. BIOL. CHEM. (Tokyo) 30: 149-154.

SHIN, M.; NAKAMURA, W. 1962. Indoleacetic acid oxidase activity of wheat peroxidase. J. BIOCHEM. 52: 444-451.

SIEGEL, B.Z.; GALSTON, A.W. 1967. Indoleacetic acid oxidase activity of apoperoxidase. SCIENCE 157: 1557-1559.

SIEGEL, S.M. 1956. The chemistry and physiology of lignin formation. QUART. REV. BIOL. 31: 1-18.

SIEGEL, S.M. 1956. The biosynthesis of lignin; evidence for the participation of cellulose as sites for oxidative polymerization of eugenol. 1. AMER. CHEM. SOc. 78: 1753-1755.

SIEGEL, S.M. 1957. Non-enzymatic macromolecules as matrices in biological synthesis. The role of polysaccharides in peroxidase catalyzed lignin polymer formation from eugenol. J. AMER. CHEM. SOc. 79: 1628-1632.

SIEGEL, S.M.; GALSTON, A.W. 1955. Peroxide genesis in plant tissues and its relation to indoleacetic acid destruction. ARCH. BIOCHEM. BIOPHYS. 54: 102-113.

STEEN, D.A.; CHADWICK, A.W. 1973. Effects of cycloheximide on indoleacetic acid-induced ethylene production in pea root tips. PLANT PHYSIOL. 52: 171-173.

STRIKLAND, E.H.; KAY, E.; SHANNON, L.M.; HORWITZ, J. 1968. Peroxidase isoenzymes from horseradish roots. III. Circular dichroism of isoenzymes and apoisoenzymes. J. BIOL. CHEM. 243: 3560-3565.

SWEDIN, B.; THEORELL, H. 1940. Dioximaleic acid oxidase action of peroxidases. NATURE. 145: 71-72.

BIOCHEMISTRy 59

TAUBER, AT.; BABIOR, B.M. 1977. Evidence for hydroxyl radical production by human neutrophils. J. CLIN. INVEST. 60: 374-379.

T AUBER, AI.; BABIOR, B.M. 1978. O2- and host defense: the

production and fate of O ' in neutrophils. PHYTOCHEM.2

PHOTOBIOL. 28: 701-709. THEORELL, H. 1942. The preparation and sorne properties of

crystalline horseradish peroxidase. ARK. KEMI. MIN. GEOL. A 16-: 1-11.

THEORELL, H. 1942. Crystalline peroxidase. ENZYMOLOGIA 10: 250-252.

THEORELL, H. 1947. Heme-linked groups and more of action of sorne hemoproteins. ADVAN. ENZYMOL. 7: 265-303.

VAN FLEET, D.S. 1959. Analysis of the histochemical localization of peroxidase related to the difTerentiation of plant tissues. CAN. 1. BOT. 37: 449-458.

WARDROP, A.B.; BLAND, D.E. 1959. Process of lignification in woody plants. In 'BIOCHEMISTY OF WOOD'. Kratzl, K.; Billek, G. (Eds). Pergamon Press, London, pp. 92-116.

WEISS, S.J.; KING, G.W.; LOBUGLIO, AF. 1977. Evidence for hydroxyl radical generation by human monocytes. J. CLIN. INVEST. 60: 370-373.

WITTENBERG, J.B.; NOBLE, R.W.; WITTENBERG, B.A.; ANTONINl, E.; BRUNORI, M.; WYMAN, J. 1967. Studies on the equilibria and kinetics of the reactions of peroxidase with ligands. II. The reaction of ferroperoxidase with oxygen. J. BIOL. CHEM. 242: 626-634.

y AMAZAKl, 1. 1958. PROC. INTERN. SYMPOSIUM ON ENZYME CHEM., Tokyo and Kyoto, 1947, Maruzen, Tokyo, p. 224.

YAMAZAKI, 1.; MASON, H.S.; PIETTE, L. 1960. Identification, by electron paramagnetic resonance spectroscopy, of free radicals generated from substrates by peroxidase. J. BIOL. CHEM. 235: 2444-2449.

YAMAZAKI, 1.; PIETTE, L.H. 1963. The mechanism of aerobic oxidase reaction catalysed by peroxidase. BIOCHEM. BIOPHYS. ACTA 77: 47-64.

YAMAZAKI, 1.; SOUZU, H. 1960. The mechanism of indoleacetic acid oxidase reaction catalysed by turnip peroxidase. ARCH. BlOCHEM. BIOPHYS. 86: 294-301.


y AMAZAKI, 1.; YAMAZAKI, H.; TAMURA, M.; OHNISH1, T.; NAKAMURA, S.; IYANAGI, T. 1968. Analysis of the O

2 reduction process of the peroxidase system. ADV. CHEM. SER. 77: 290-306.

y AMAZAKI, 1.; YOKOTA, K. 1965. Conversion offerrous peroxidase into compound III in the presence of NADH. BIOCHEM. BIOPHYS. RES. COMM. 19: 249-254.

YAMAZAKI, 1.; YOKOTA, K; NAKAJIMA, R. 1965. Amechanism and model of peroxidase-oxidase reaction. In 'OXIDASE AND RELATED REDOX SYSTEMS'. King, Mason and Morrison (Eds). John Wiley, New York, vol. 1, pp. 485-513.

YAMAZAKI, 1.; YOKOTA, K; TAMURA, M. 1966. In 'HEMES AND HEMOPROTEINS'. Chance, B.; Estabrouk, R.W.; Yonetani, T.(Eds). Academie Press, New York, p. 319.

YANG, S.F. 1968. Biosynthesis of ethylene. In 'BIOCHEMISTRY AND PHYSIOLOGY OF PLANT GROWTH SUBSTANCES'. Wightman, F.; Setterfield, G. (Eds). The Runge Press, Ottawa, Canada, pp. 1217-1228.

YOKOTA, K.; YAMAZAKI, 1. 1965. Reaction of peroxidase with reduced nicotinamide - adenine dinucleotide and reduced nicotinamide - adenine dinucleotide phosphate. BIOCHIM. BIOPHYS. ACTA. 105: 301-312.

ZAPROMETOV, M.N. 1978. Enzymology and regulation of the synthesis of polyphenols in cultured cells. In 'FRONTIERS OF PLANT TISSUE CULTURE 1978'. Thorpe, T.A. (Ed.). University of Calgary Press, Calgary, Canada, pp. 335-343.

CHAPTER 3

ISOPEROXIDASES : FACT OR FICTION?

The large number of peroxidase 'isoforms' appearing in most plants examined casts a certain amount of doubt as to them being native molecules. The actual number obtained is dependent largely on the separation techniques used (Brewbaker et al., 1968; 280; 584; 585; 738; 803). This, therefore, makes comparison of results from different laboratories very difficult. Thus the non-initiated reader of a peroxidase paper must be aware of the main factors causing this variation.

Buffer extractibility

The nature of the buffer used, its ionic strength, and its pH affect the peroxidase recovery both quantitatively and qualitatively (Adatthody and Racusen, 1967; Gaspar et al., 1969; 510; 796). Part of the explanation certainly lies in the relative buffer solubilization capacity for the (natural or artificiai) enzyme ionic association to cell organelles and the wall. It certainly can be said that most peroxidase extractions reported in papers dealing with plant physiological problems are imperfect.


Extract manipulation, binding to organelles

The above statement also may explain the modifications in number, intensity, size and aggregation properties, and migration speed of peroxidases (304, 10 17, 1258) due to in vitro manipulations of the extracts. Besides this differential release of cellular, intercellular and organelle-bound peroxidases, the partial 'solubility' or 'pelletability' of organelles indeed has to be taken into account in the crude or even purified extracts. As an exemple, it has been demonstrated that peroxidases appearing with an abnormally high molecular weight with the peak of proteins after Sephadex (G-100 or G-200) filtration (Cronenberger et al., 1966; Gaspar et al., 1969; Weber, 1970; 280, 610) were basic peroxidases apparently not different from those of the second peak with a normal molecular weight : they simply had been filtrated through Sephadex with the membrane structures on which they were attached (282). Darimont and Baxter (279) state that such membrane structures are still present in ribosomes and mitochondriaenriched preparations which renders the identification of the specifie organelle-attached peroxidases uncertain. Peroxidases can be detached from membrane structures in vitro and further reassociated with the specifie aid of the calcium ion (1016).

It can be added also that the visualization of isoperoxidases in gels is strongly influenced by the substrate concentration (Novacky and Hampton, 1968), the pH of incubation and the hydrogen donor used for the image enhancement (370, 651, 723).

Inhibitors, binding to phenolics, interconversion

The control of peroxidase activity through physical or chemical factors may of course pass through repression or derepression of genes leading to de novo synthesis (Galston et al., 1968; 1175) but it can also be the result of activation of preformed inactive enzyme molecules (Zucker, 1972) or mediated by non-protein effectors, mainly of a

ISOPEROXIDASES 63

phenolic nature (Gaspar, 1965; Dinant and Gaspar, 1967; 387, 619, 745, 1385, 1386). Peroxidase of Cichorium intybus is under the photocontrol of phenolic inhibitors and sorne isoperoxidases submitted to electrofocussing may migrate together with inhibitors (749). It is possible that such an association exists in vivo (1002).

Following the disruption ofplant-cell organization, cellular phenolics may be oxidized by phenol oxidase (Sheen and Calvert, 1969) or peroxidase(Sheen, 1969) to quinones, condensed tannins, and ultimately

i'·:'· to brown pigments (Webb, 1966). Many examples are cited in the literature showing that phenolics inhibit various enzymes during their extraction from plant tissues (Anderson, 1966; Loomis and Battaile, 1966; Walker, 1980). A report from Fieldes and Tyson (387) suggested a phenolic-peroxidase interaction during the extraction of the enzyme from flax tissues. Data from Srivastava and Van Huystee (1257) suggest that treatment with Dowex l-X l, which removes phenolics from proteins, converts five anodic isoperoxidases into a single one. A same result is obtained with albumin and cystein (1378). Along the same line, Penel et al. (1017) found that a peroxidase from lentil root may be transformed into several peaks after addition of a boiled extract. As a general rule, it is advisable to remove phenolics from an extract before the separation of peroxidases by electrophoresis. For this purpose, many reducing or absorbent chemicals such as carbowax (1391), ascorbic acid and/or cystein (499), insoluble polyvinylpyrollidone (Jones et al., 1965; Castillo et al., 1981; 440, 510), collagen and casein dispersion (500), etc., have been used. It is understandable, therefore, that the physiological meaning of measurements made from such extracts is subject to discussion. Effectors may have as an important regulatory role as the enzyme activity per se. This seems to be particularly the case for the so-called auxin-protectors (Rethore et al., 1974; Kevers et al., 1981 a and b; 134, 137,436,955, 1305, 127, 1281).

Changes in number or properties of isoperoxidases have also been reported fol1owing heat treatment (304), storage (1158), gel chromatography at room temperature (616, 10 17) or incubation at increasing pH (768). Recently, Decedue and Borchert (1980) claimed that it is possible to convert the various isoperoxidases from potato into a single electrophoretic species. This was obtained after chromatography of potato juice in a column of Sephadex G-IOO. in the presence of 2 M CaCI

2 "


It thus appears from the literature that the numerous isoperoxidases may be the product of interaction of a: few or even a single isoform with other molecules. In addition, according to the method of separation, the same biological material may exhibit a variable number of isoperoxidases. For example, a separation of an extract from spinach leaves yields nine bands after acrylamide gel electrophoresis, ten bands with column isoelectric focusing, fifteen after isoelectric focusing in acrylamide gel and up to sixteen bands after starch gel electrophoresis (Pene!, 1976; 658). It was also reported that a single peak collected after column isoelectric focusing may be resolved into several bands by starch gel electrophoresis (Darimont, 1977).

Peroxidase-like activity

Other sources of misinterpretations have come from the state'ment that peroxidase also display phenoloxidase activity and that other hemecontaining molecules also catalyze the decomposition of hydrogen peroxide and consequently the oxidation of classical peroxidase substrates (Saunders et al., 1964). The apparent identity of polyphenoloxidases and peroxidases revealed with sorne substrates has been discussed by Van Loon (1393), who has developed a specific staining method indicating non-identity with peroxidases.

Several isozymes from peanut cells in suspension medium however possess peroxidase, IAA-oxidase and polyphenol oxidase activities (1255, 1257). The studies on the active site revealed that polyphenol oxidase and IAA-oxidase share the same active site on the apoenzyme (1257). Catalase is even able to function as IAA-oxidase (Avelia et al., 1966). An additional source of error, when interpreting a peroxidase zymogram, is the presence of cytochrome c which oxidizes guaiacol in the presence of HzOz and shows three distinct bands of activity after starch gel electrophoresis (434).

65 ISOPEROXIDASES

Cellular redistribution

Apparent absence of visible changes in peroxidases relative to sorne particular phenomenon does not necessarily ref1ect the in vivo situation. It has already been mentioned that possible release as soluble peroxidases in the extracts of enzymes attached to organelles, by simple ionic exchange due to buffers or by chelation, may occur. Fractionation of extracts (with similar total enzyme activity) of different plants (133, 143, 1016, 1024) sometimes indicates a cellular redistribution of peroxidases. This may or may not be associated with qualitative and quantitative changes taking place in the course of sorne physiological process. Thus, e.g., in vitro far-red and red irradiations of extracts of spinach Ieaves modify the pelletability of peroxidase activity (\0\9). These findings may render the comparison of results from different sources more difficult and their interpretation doubtful.

Immunochemical and peptide mapping studies

In order to solve the problem of the existence of several distinct forros of peroxidases, two techniques are feasible. The first one is the immunochemical study of peroxidases. The second one is the comparison of tryptic peptide maps or the elucidation of the complete amino-acid sequence. There are only few reports concerning immunochemical characteristic of peroxidase proteins. Bakardjieva and Georgiev (58) showed that the peroxidase function in plants at different phylogenetic positions may be realized by proteins differing in immunochemical and serological properties. However, there is sorne antigenic similarity among sorne plant species such as horseradish, pea, maize and barley, but this similarity was not observed for aIl the peroxidase isoenzymes.

According to Cairns et al., (182) different peroxidase isoenzymes from peanut Ieaves, peanut cells and peanut suspension cell medium share cornmon antigenic deterroinants. There is also an immunological relatedness between peanut and a horseradish peroxidase. These results suggest an evolutionary conservatism in peroxidase structure. There is however sorne reports on the distinct antigenic specificities of


isoperoxidases in the same organism. Such data were reported by Daussant el al. (287) in Datura stramonium and by Kahlem (645) in Merclirialis annua.

The tryptic digestion of apoperoxidases gives peptides which can be separated by two-dimensional electrophoresis. After staining, a peptide map is obtained, which is characteristic of a protein. The comparison of such maps is a mean of comparing the degree of similarity between two proteins. This technique was used by several authors. Shih et al. (1208) found that horseradish peroxidase isoenzymes could be segregated into at least three distinct groups and it appeared that there are many points of difference in the primary structure among the three groups. In turnip root (1425), the two most acidic peroxidases only differ significantly in one peptide and a third one is related to these two. Horseradish isoperoxidase c also belongs to this group. But the most cathodic peroxidase of turnip differs from this group, at least around two disulfide bridges, and therefore, probably was different from the other four in parts of its three dimensional structure. From this study, it appears that each peroxidase contains two highly homologous sequences.

In tobacco tissue culture eight isoperoxidases have been subjected to trypsin digestion followed by peptide mapping. The peptide maps of two of them were identical and ail the other isoperoxidases did not appear to be dramatically dissimilar in certain portions oftheir sequence, since many matching peptides were found when various isoperoxidases were cross-compared. However, only two or three highly homologous peptides were present in ail of the isoperoxidases. It therefore appears that at least sorne portions of the peptides which include active sites have been conserved among ail isoperoxidases from tobacco (680).

Tomato peroxidase can be resolved into two non-identical subunits in the presence of dithiothreitol, while horseradish peroxidase remains as a single polypeptide chain after such treatment (697). Tobacco isoperoxidases G 1 were also unaffected by a similar treatment (802).

It is thus difficult to know whether the numerous bands ofperoxidase activity obtained by electrophoresis correspond to distinct proteins or are conformers or degradative forms of one or two molecules. Much work needs to be done in this area. Resolution of sorne of the above problems will go a long way in establishing the structural authenticity of isoperoxidases.

ISOPEROXIDASES 67

REFERENCES

For numbered reJerences in the text, see bibliographical section

ADATTHODY, K.K.; RACUSEN, D. 1967. On the extraction of peroxidase isozymes from bean leaves. CAN. J. BOT. 45: 2237-2242.

ANDERSON, J.W. 1966. Extraction of enzymes and subcellular organelles from plant tissues. PHYTOCHEM. 7: 1973-1988.

AVELLA, T.; DINANT, M.; GASPAR, Th. 1966. Action des acides 0-, m-, et p-hydroxybenzoiques sur la destruction de l'acide 13indolylacétique par la catalase de foie de boeuf. BULL. SOc. ROY. Sc. LIEGE 35: 307-314.

BREWBAKER, J.L.; UPADHYA, M.D.; MAEKINEN, Y.; MACDONALD, T. 1968. Isoenzyme polymorphism in flowering plants. III. Gel electrophoretic methods and applications. PHYSIOL. PLANT. 21: 930-940.

CASTILLO, F.J.; PENEL, c.; GASPAR, Th.; GREPPIN, H. 1981. Masquage et démasquage des isoperoxydases de Pelargonium. C.R. ACAD. Sc. PARIS 292: 259-262.

CRONENBERGER, L.; VILLE, R.; PACHECO, H. 1966. Purification partielle des auxine-oxydases des racines de Pisum sativum. BULL. SOc. CHIM. BIOL. 48: 833-836.

DARIMONT, E. 1977. Les peroxydases de la racine de lentille. Leur variation en rapport avec l'interaction auxine-cytokinine sur la croissance. Thèse de doctorat, Univ. Liège, 223 p.

DECEDUE, c.J.; BORCHERT, R. 1980. Potato peroxidase isozymes. PLANT PHYSIOL. 65 (suppl.): 29.

DINANT, M.; GASPAR, Th. 1967. Acide 13-indolylacétique-oxydase, peroxydase, catalase, phénoloxydase et effecteurs naturels chez Phaseolus vulgaris cultivé à l'obscurité et à la lumière. BULL. SOc. ROY. BOT. BELG. 100: 73-94.

GALSTON, A. W.; LAVEE, S.; SIEGEL, B.Z. 1968. The induction and repression of peroxidase isozymes by 3-indoleacetic acid. ln 'BIOCHEMISTRY AND PHYSIOLOGY OF PLANT GROWTH SUBSTANCES'. Wightman, F.; Setterfield, G. (Eds). The Runge Press, Ottawa, Canada, pp. 445-472.


GASPAR, Th. 1965. Catabolisme auxinique et effecteurs auxinesoxydasiques. Etude comparée chez Lens culinaris et Salvia splendens. BULL. SOc. ROY. Sc. LIEGE 34: 391-537.

GASPAR, Th.; LACOPPE, J.; HOFINGER, M. 1969. Influence de la nature, du pH et de la force ionique du tampon d'extraction dans la mesure des activités peroxydasique et catalasique des racines de Lentille. BULL. SOc. ROY. BOT. BELG. 103: 207-211.

JONES, J.O.; HULME, A.c.; WOOLTORTON, L.S.c. 1965. The use of polyvinylpyrrolidone in the isolation of enzymes from apple fruits. PHYTOCHEM. 4: 659-676.

KEVERS, c.; COUMANS, M.; DE GREEF, V.; HOFINGER, M.; GASPAR, Th. 1981a. Habituation in sugarbeet callus: auxin content, auxin protectors, peroxidase pattern and inhibitors. PHYSIOL. PLANT. 51: 281-286.

KEVERS, c.; COU MANS, M.; DE GREEF, V.; JACOBS, M.; GASPAR, Th. 1981 b. Organogenesis in habituated sugarbeet calius: auxin content and protectors. Peroxidase pattern and inhibitors. Z. PFLANZENPHYSIOL. 101: 79-87.

LOOMIS, W.D.; BATTAILE, J. 1966. Plant phenolic compounds and the isolation of plant enzymes. PYHTOCHEM. 5: 423-438.

NOVACKY, A.; HAMPTON, R.E. 1968. The effect of substrate concentration on the visualization of isoperoxidases in dise electrophoresis. PHYTOCHEM. 7: 1143-1145.

PENEL, C. 1976. Activité peroxydasique et développement chez Spinacia oleracea. Thèse de doctorat No. 1667, Univ. Genève, 160 p.

RETHORE, J.L.; GAS, G.; FALLOT, J. 1974. Les substances de type 'protecteurs d'auxine' des explantats de parenchyme vasculaire de Topinambour: libération et évolution dans le milieu de culture. C.R. ACAD. Sc. PARIS 279: 153-156.

SAUNDERS, B.C.; HOLMES-SIEDLE, A.G.; STARK, P.B. 1964. Peroxidase. Butterworths, London, 27 J p.

SHEEN, S.J. 1969. The distribution of polyphenols, chlorogenic acid oxidase and peroxidase in different plant parts of tobacco, Nicotiana tabacum L. PHYTOCHEM. 8: 1839-1847.

SHEEN, S.J.; CALVERT, J. 1969. Studies on polyphenol content, activities and isozymes of PPO and peroxidase during air curing in three tobacco types. PLANT PHYSIOL. 44: 199-204.

::~::~~:

ISO PEROXIbASES 69

WALKER, J.R.L. 1980. Enzyme isolation from plants and the phenolic problem. WHAT'S NEW IN PLANT PHYSIOL. 11: 33-36.

WEBB, J.L. 1966. Enzymes and metabolic inhibitors. ln 'QUINONES'. Webb, J.L. (Ed.). Academie Press, New York, pp. 43 1-594.

WEBER, J.A. 1970. Sorne aspects of growth regulation in plants. Ph.D. Thesis, Univ. Utrecht, 80 p.

ZUCKER, M. 1972. Light and enzymes. ANN. REV. PLANT PHYSIOL. 23: 133-156.

· .... ,

CHAPTER 4

PEROXIDASES AT THE SUBCELLULAR LEVEL, THEIR BIOSYNTHESIS AND

ITS REGULATION

4.1. CELLULAR LOCALIZATION OF PEROXIDASES

4.1.1. Technical aspects

Peroxidase activity is easily localized by light and electron microscopy. The electron donor commonly used for this purpose is 3,3'-diamino-benzidine (DAB), which was introduced by Graham and Karnovski (1966). Other reagents have been used; these include pphenylene diamine (1065), benzidine (Van Duijn, 1955), tetramethylbenzidine (866, 867), o-dianisidine (314), 3-amino-9-ethylcarbazole (Graham et al., 1965), 2,5- or 2,7-fluorene-diamine (970) and homovanillic acid (989). Syringaldazine has also been used, especially to study the involvement of peroxidases in the process of lignification (l90a, 191, 525). DAB, which gives a precise and strong staining reaction appears to be the most suitable reagent for peroxidase staining of tissues and ceIls. lt has the advantage that, in the presence of hydrogen peroxide and peroxidases, it produces an osmiophilic polymer, which is insoluble after post-fixation by osmium tetraoxide. The DAB technique is very simple, but care must be taken to work under


conditions (pH, temperature, H20

2 concentration, percent aldehyde for

fixation) in which only peroxidases, and not other hemoproteins such ascatalaseorcytochromescan react(376, 559,1118,1216,1289,1421).

The penetration of the staining medium is dependent on the thickness of the tissue section. Incubation with thin sections allows good penetration of the DAB reagents, but it leads to a considerable loss of the enzyme into the medium (514). There is therefore a 10ss of the activity. However, this loss can be reduced by a suitable prefixation of the tissue with glutaraldehyde. Other possible sources of artifacts should be mentioned. On one hand when organs or pieces of tissue are cut, cellular redistribution of peroxidases may occur before the fixation process is achieved, since mechanical injury can induce a release of peroxidases out of cells. On the other hand, sorne peroxidases are free in the cytoplasm (467) and in the walls and intercellular spaces (see table 1). They can diffuse and be absorbed in a non specific manner when cells are disrupted by cutting. Several isoperoxidases have a high isoelectric point and can interact with negatively charged structures, such as walls, membranes or ribosomes.

Despite these possible artifacts, which can lead to misleading conclusions, cytochemical observations remain the best method of studying cellular localization of peroxidases. Cell fractionation, the other available method, give results which must be assessed with extreme caution. The disruption of ceIls, indeed, mixes ail the cell components and many non-specific interactions between peroxidases and various cellular structures and molecules can occur. From this point of view, reports on the presence of high peroxidase activity on isolated ribosomes must be accepted with cautions (Matsushita and Ibuki, 1960; 279, 1028).

In the same way, the level of peroxidase activity ionically-bound to wall material in extracts, which is sometimes presented as having a physiological meaning, is probably in part a reflection of the capacity of cell walls to absorb solubilized peroxidases. There is however an alternative technique available if one wishes to quantify the peroxidase activity actually present in the wall and in the intercellular spaces. This is the vacuum infiltration of a liquid into the plant tissue, followed by the recovery of the fluid by centrifugation. This method was introduced by Abeles and Leather (1971) and was applied to peroxidases by Stafford and Bravinder-Bree (1262) (see also Castillo et al., 1981; 115, 153, 801, 870, 1077). This method, which does not affect the

73 LOCALIZATIaN AND BIOSYNTHESIS

protoplasts (protoplasts means here cells without wall in situ) has the additional advantage that the ionic strength of the infiltration medium can be chosen in such a way as to withdraw either free or ionicallybound peroxidases from the tissues. This was done by Miider (801) who found three distinct groups of isoperoxidases present in the wall : one which moves freely and can be extracted with water, a second one ionically-bound and a third one which is covalently-bound. This technique may also provide valuable information on the rate of release of peroxidases out ofthe protoplast in relation to any chosen physiological process (153).

As far as peroxidases of the isolated protoplast are concemed, it is possible to separate the enzymes enclosed in a membranous structure, provided that an appropriate extraction technique is used (mild grinding, high osmolarity of the extraction buffer). This has been done for vacuolar peroxidases (486).

4.1.2. Cellular localization

It is useful to keep in mind all the technical reservations mentioned above when considering results conceming the cellular localizations of peroxidases. Table 1 summarizes the various plant cell parts which have been reported to exhibit sorne peroxidase activity. This is by no way an exhaustive list orthe papers that have appeared on this subject.

Several questions arise when interpreting the numerous locations of peroxidases at the cellular level. Is it possible that such reactive enzymes are so widely distributed within plant cells ? Do artifacts play a part in this distribution? It is not easy to answer these questions.

The presence of peroxidase in the cell wall is not a matter of controversy. Cytochemical observations and vacuum infiltration of (active) tissues provide sufficient evidence that cells release peroxidases towards the extracellular spaces and that these enzymes remain active. There are also indications that wall peroxidases partially differ from protoplast peroxidases (153, 801). The existence of extracellular peroxidases is also demonstrated in cell suspension cultures.


More difficult to interpret is the localization of peroxidases within the cell. There is little doubt that they are present in cistemae and vesic1es of the Golgi apparatus, in small and central vacuoles and in the endoplasmic reticulum. These localizations are apparentJy not artifacts, since in these cases, the reaction product of DAB oxidation is localized inside the closed membranes. It should be noted however, that cytochrome P450, which is associated with the endoplasmic reticulum, can exhibit peroxidase activity (1091, 1092). Vacuole peroxidases have been observed by cytochemical techniques and after cell fractionation. For example, Grob and Matile (486) reported that in horseradish root, over 70 percent of the peroxidase activity is contained in central vacuoles. Other reports on the presence of peroxidase on the plasmalemma, on ribosomes and on nuc1ear components should be reevaluated for the reason that all these cell structures carry many negative charges and could trap peroxidase which diffuse after tissue cutting.

Mitochondria and chloroplasts sometimes have been reported to contain appreciable amounts of peroxidase. These localizations were observed after separation of the cell components by density gradient centrifugation. Cytochemical studies do not confirm these Jocalizations which probably are due to contamination of chloroplast or mitochondria fractions with other cell components (Pleniscar et al.,1967).

The overall conc1usion which can be drawn from the available literature is that peroxidase activity is mainly associated with the endocellular membrane system and the cell wall. The consequence of this localization concerning both the biosynthesis of the enzyme and its possible physiological fractions will be discussed later. However, it is evident that every localization, revealed in the presence of exogenously supplied hydrogen peroxide, does not necessarily correspond to a site where peroxidases exert their function in vivo. Endogenous hydrogen peroxide most likely acts as a limiting factor which can control to sorne extent peroxidase activity.

The cellular localization of peroxidase has been intensively studied also in animal celIs, especially in sorne specialized mammalian cells. Peroxidases have been found in parotid and submaxillary glands (560, 957, 1296), in lacrimal glands (561: 562), in mammary glands (28), in uterine epithelium (227, 794). AlI these organs have in common the property of secreting fluid, in which peroxidases are thought to exert an antimicrobial role. In addition, peroxidases have been found

LOCALIZATION AND BlOSYNTHESIS 75

in leukocytes (381, 1291), eosinophils (634, 635, 873), heterophils (318) and macrophages (1001), mamrnary tumor cells (316, 317, 341), thyroid epithelial cells (272, 959), etc. In almost every case, a study of the intracellular localization of peroxidase with the aid ofelectron microscopy showed the presence of these enzymes in the endoplasmic reticulurn (often including the nuclear envelope), in elements of Golgi apparatus and in secretory granules. These cellular localizations imply that peroxidases are exportable proteins; however, in sorne cases (thyroid or Kuppfer cells of rat liver) they have been shown to be integral membrane proteins (375, 1080).

A comparison between plants and animaIs shows therefore a great sirnilarity in the subcellular localization of peroxidases. As it is in the case in animaIs, peroxidases do not appear in every plant cell type. We may say that the localization of peroxidases in plants varies with seasons (Czaninski and Catesson, 1969), with species, with the degree of differentiation and that the subcellular distribution is different in each tissue (Poux, 1969; 190a, 191).

For example, peroxidase staining is particularly strong in the root cap, epidermis, inner cortex and pith in Pisum (Poux, 1969; 391, 392); in phloern and maturing xylem (514); in the epidermis, hypodermis, endodermis and sorne parenchyrna cells of hypocotyls of e.g., Phaseolus (\939); and in sieve and parenchyma cells of cotton (191). Sorne cells appear devoid of peroxidase activity, e.g., the cortical band and xylem tissue of Pisum root (391, 392). In fully-expanded spinach leaves extracellular peroxidase seems to be mainly located in small vascular tissues, as it is the case in the young leaves of Vanda (Alvarez and King, 1969). In the same organ, e.g., a root, the subcellular localization of peroxidase differs from tissue to tissue and in the same tissue from cell to cell.

A source of error during the histo- and cytochemical study of peroxidase in plants, which is never discussed by the authors, is the presence of many inhibitors of peroxidase activity. These inhibitors, mainly of a phenolic nature, are often shown to be capable of masking the activity of peroxidase in plant extracts (436, 684). It can be assumed that they also interfere with the peroxidase reaction during the staining procedures and furthermore the phenolic content of each tissue is probably different.


Table 1: Localization of peroxidases in higher plant cells.

Techniques of detection

Compartments

Cell wall

Plasmalemma

Cytoplasm

Golgi apparatus

Light or electron microscopy

Van Fleet, 1959; De Jong 1967; Poux, 1969; 161, 188, 191, 514, 515,993,1065, 1399,1420, 1480

Poux, 1969; 191, 467, 1420

467

Poux, 1969; 110, 161, 191, 265, 467, 514, 1480

Cell fractionation

115, 134, 188, 283, 391, 392, 440, 496, 739,801,804,1109, 1262

739, 1023

739, 1442

Secretory 467, 1480 vacuoles

LOCALIZATION AND BIOSYNTHESIS 77

Small vacuoles Poux, 1969; 253 191, 265, 467, 514, 993, 1052, 1053

Central vacuole and tonoplast

Rough endoplasmic reticulum

Bound ribosomes

Free ribosomes

Chloroplasts

Chromosomes

Nucleoles

Poux, 1969; 110, 188, 265, 1420

Poux, 1969; 188, 191, 265, 467, 514, 544, 1420

467, 1480

191, 467

1065

1065

124, 486, 993, 994

1024

Matsushita and Ibuki, 1960; 279, 428, 739, 919, 1028

613, 919


It is also weil known that the peroxidase activity of a whole plant or a plant organ may be resolved into several isoforms by electrophoresis (see Chapter 3). The question that arises is whether an isoperoxidase corresponds to a particular localization in the cell or is specifie to one kind of cell. This problem is not yet resolved. Mader and coworkers (804, 805, 806) showed that in tobacco tissue cultures a fast migrating anodic isoperoxidase moves freely in the cell wall and intercellular spaces and is not present in the naked protoplast, while the two other groups of isoperoxidases (slow migrating anodic group and slow migrating cathodic group) are mainly located in the protoplast, and are respectively covalently and ionically-bound to the wall.

Histoimmunology was used by Kahlem (465) to localize three isoperoxidases which were specifie for male flowers of Mercurialis annua. For that purpose, the specifie isoperoxidases were purified and injected into rabbits. The resulting serum was used to 10calize the 'male' isoenzyme and it was shown that this isoenzyme only occurred in the stamen and particularly in sporogenous tissue and the tapetum. This kind of approach would be very useful not only to precisely localize each isoperoxidase within the tissue and even within the cell, but also to study the biosynthesis of isoperoxidases as was done in Mercurialis. The results obtained by immunodetection wouId be more reliable than those obtained after cell fractionation.


4.2. BIOSYNTHESIS OF PEROXIDASES AND ITS

REGULATION

4.2.1. De novo synthesis or activation

Peroxidases were used as marker enzymes for the study of numerous physiological processes, as weil as for testing the effect of several chemical substances on plant cells. They also strongly respond to changes in the environmental conditions, to infectious agents (virus, bacteria, fungi), and to injuries. Ali these factors affect peroxidases either by changing their activity (perhaps more correctly their measured capacity) or by changing the number of isoforms which can be discriminated by electrophoresis. The variation of activity results either from an inactivation or activation of preexisting molecules, from a change in the rate of synthesis of the enzymes, or from the transfer of peroxidases from one cell compartment to another. Most studies do not provide any information on this point, but only report on changes of peroxidase activity measured in more or less crude extracts.

Before going through the various steps in the control of the level of peroxidase activity in plants, it must be stated that the simple measure of peroxidase activity in crude extracts often is a misleading reflection of the actual number of peroxidase molecules really present in the tissue before extraction. Plant ceIls, indeed, contain several substances (phenolics and others) which modify the ability of peroxidases to oxidize the electron donors generally used to detect their activity. These compounds, which probably are separated from peroxidases in whole ceIls as a result of different compartmentalization, are mixed with the enzymes when cells are broken and interact with the enzymes during the assay.

A striking example of this difficulty is provided by studies using Pelargonium (Castillo et al., 1981). Leaves or petioles of this plant, when ground in a buffer according to the procedures commonly used for the extraction of peroxidases, do not exhibit any peroxidase activity as shown previously (Lavee and Galston, 1968; 436). However, the conclusion that this organ fails to contain peroxidase is not correct,


since the intercellular fluid collected by centrifugation after vacuum infiltration exhibits very strong peroxidase activity. In this case it was shown that the protoplast contained inhibiting and reducing substances which, once mixed with the extracellu1ar peroxidase after grinding of the organs, comp1etely mask this activity. This artefact can be overcome by use of insoluble polyvinylpyrrolidone, which traps the phenolic inhibitors (Jones et al., 1965).

It isevident from this examp1e that changes occurring in peroxidase activity, fol1owing a change in the environment of cells, could be due to the appearance or disappearance of inhibitors or activators. It could also be due to a modification of transcription of RNA or of translation of apoperoxidase. These steps can be studied by use of specific inhibitors (Kanazawa et al., 1965; Gayler and Glasziou, 1968; Gahagan et al., 1968; 954, 1108, 1190, 1315, 1381). Deuterium oxide used for density labelling (Siegel and Galston, 1966; 30) or radioactively labelled amino acids or sugars (1190, 1376) may a1so provide information about the rate of peroxidase biosynthesis. Excised plant tissues are particularly suitable for such studies. As a matter of fact, most tissues react to injury or excision by an enhancement of their peroxidase activity (Bastin, 1968).

4.2.2. Transcription

In sugar-cane stalk tissues (Gay1er and Glasziou, 1968) and excised lentil embryonic axis (674), both 6-methylpurine and actinomycin D reduce the increase of peroxidase activity which normally fol1ows excision. By using these inhibitors and low temperature, the authors were able to determine that the half-life for peroxidase rn-RNA decays was 1.5 hour for sugar-cane and 3 hours for lentil. On the contrary the stimulation of peroxidase activity in excised wheat embryos cultured for 48 hours was not affected by actinomycin D, although the inhibition of new RNA synthesis was effective (1315). This therefore indicates that there may be conserved messengers for peroxidases, which are capable of supporting peroxidase synthesis under conditions of strong inhibition of RNA synthesis. The comparison between these two examples shows that the life of messenger RNA for peroxidase may be extreme1y variable.

81 LOCALIZATION AND BIOSYNTHESIS

This fact makes the study of the control of peroxidase synthesis at the transcriptional level very difficult. The efTects of actinomycin D were assayed in several systems. It was found to inhibit the peroxidase stimulation induced by ethylene or injury in tobacco pith (115, 753), sweet potato (Kanazawa et al., 1965, Gahagan et al., 1968), and pea seedlings (1108). In cultured peanut cells, actinomycin D has an inhibiting efTect only during a brief time following the lag phase of growth (1381). But there are also several reports showing either no efTect of this inhibitor (115) or even a stimulating efTect. The paradoxical stimulation of peroxidase production was observed in oat leaves (954), in potato roots (115) and in pea epicotyls (1108). In pea epicotyl tissue, actinomycin D exerts its paradoxical efTect only when given after ethylene. Ridge and Osborne (1108) suggested that it may enhance the level of peroxidase by blocking the synthesis or the action ·of specific inhibitors which inactivate the enzyme or prevent its translation from a stable rn-RNA template. An alternative explanation would be that actinomycin D induces a non-specific response at a posttranscriptional level.

4.2.3. Translation

ln contrast to actinomycin D efTects, inhibitors of protein synthesis give unambiguous results when applied to plant tissue. However, in one case, it was reported that cycloheximide enhances peroxidase activity (1194). There are several examples showing that the stimulation of peroxidase activity may be abolished by cycloheximide, blasticidin S or other translation inhibitors. Ethylene (Gahagan et al., 1968; 1108), injury (674, 1190), germination (1315), deetiolation (1194) and infection (1371) are factors inducing a marked increase of peroxidase activity which can be inhibited or diminished by such inhibitors. It is thus likely that plant cells can control their peroxidase activity by changing the rate of synthesis of peroxidase molecules. Another mode of control may involve RNA as part of a repressor activity. Such a RNA fraction is present in intact tobacco pith or in excised pith treated with IAA (753). When applied to excised pith, it inhibits the appearance of the new isoperoxidases due to excision.


In peanut cell suspension, cycloheximide was shown to block almost completely the synthesis of protein, but did not affect the rate of peroxidase release into the medium (1382), suggesting the presence of a large reserve pool of peroxidases either within the cell or in their walls. In these cells, cycloheximide is active only after the transfer of the cells into a fresh medium (1381).

Formation of rn-RNA and synthesis of the apoprotein are two important steps in the control of peroxidase activity, but an additional key factor in this control couId be the availability of heme within the cell (1380). This availability is dependent upon porphyrin metabolism and the synthesis of other porphyrin containing molecules, such as chlorophyll and cytochromes.

4.2.4. Post-translational steps and secretion

There are further steps in the control of peroxidase activity. These post-translational controis are likely to involve severai cations. Although no clear demonstration has been made, the existence of peroxidases in an inactive state was sometimes postulated. Recent data (Sticher et al., 1981) showed that spinach celis, cultured in the absence of calcium, contained peroxidases which could be activated by calcium at millimolar concentration. Calcium-activated peroxidases were also found in Hevea root (454). It is also known that one or two calcium ions are incorporated in the apoprotein moiety of horseradish peroxidases and are absolutely necessary to the enzyme activity (531). In addition, Fielding et al. (391) reported that cell wall peroxidases of pea roots are considerably activatedd when sodium or potassium were added to the assay medium.

Finally , the transport of peroxidases towards their actual site of action may also be considered as a control of peroxidase activity by cells. Cytochemical studies have shown that the final locations of peroxidases are likely to be either cell wall and intercellular free spaces or vacuoles. An appreciable amount of activity is often detected on ribosomes bound to the endoplasmic reticulum, suggesting that they are synthetized there. Peroxidase activity on bound ribosomes was often observed in plant and animal cells, thus indicating that the


coenzyme is readily incorporated to the proteinic part of the enzyme. These peroxidases probably are transported towards the vacuoles or the cell wall, following two distinct routes. In addition, peroxidases are glycoproteins. Using affinity chromatography with concanavalin A Sepharose, Nessel and Miider (942) found that ail the isoperoxidases extracted from tobacco cel1s contained carbohydrate groups. In contrast, Van Huystee (1376) also using affinity chromatography found that sorne perQxidases from peanut cel1s did not possess the specific sugars required for an affinity with concanavalin A. Whether these peroxidases contained other sugars than mannose or are precursors for those retained on con A Sepharose was not determined by the author. In the latter case, the absence of carbohydrate would mean that the incorporation of the sugar residue occurred at a post-translational level, for example in the Golgi apparatus. Lew and Shannon (757), working with sliced root tissue of horseradish incubated in the presence of 3H-Ieucine and 14C-mannose, came to the conclusion that the synthesis of the peptide portion of peroxidase was completed before the monosaccharide residues were attached to the molecule.

In another study, Sevier and Shannon (l187a) have described a glycosyl transferase from horseradish root tissue which catalyzes the transfer of 2-acetamido-2-deoxy-D-glucose from 2-acetamido-2-deoxyD-glucose to the isoenzyme C of horseradish peroxidase. This peroxidase was previously treated with a glycosidase and is used as acceptor to study the glycosylation of protein in plants. There is no information available from the literature on -the composition of the peroxidases which are bound to ribosomes. If these peroxidases are devoid of their carbohydrate part, they are likely to be enzymes just formed on the ribosomes. But if they are already glycosylated, the hypothesis of an artifactual binding to ribosome, fol1owing cell disruption, would be probable. The data obtained by Lew and Shannon (757) and by Van Huystee (1376) suggest that the biosynthesis of peroxidases is quite similar to the biosynthesis of glycoproteins in mammalian systems. In addition, the biosynthesis and the processing of peroxidase molecules within plant cells exhibit the main characteristics of the secretory protein in animais (Palade, 1975).

We know from the work of Maccecchini, Rudin and Schatz (783a) that the apoprotein of yeart cytochrome C peroxidase is made outside the mitochondria as a larger precursor, which is then transported into mitochondria and processed to its nature form in the absence of protein


synthesis. Stephan and Van Huystee (1271) succeeded in obtaining in vitro synthesis of peroxidases with either free or membrane-bound ribosomes. The peptide obtained by the procedure had the same antigenic properties as the extra-cellular cationic peroxidase, but it had a slightly higher molecular weight. The authors concluded that the in vitro synthetized protein contained a signal peptide characteristic of secreted proteins. They also showed that the amount of peroxidases synthetized in vitro on membrane-bound polysomes was about twice as much as that on the free polysomes (Stephan and Van Huystee, 1981).

In cress root hairs, peroxidases seem to be synthetized in the endoplasmic reticulum and within dictyosome cistemae, packaged and transported in secretory vesicles and extruded into cell wall (1480). Many mammalian cells, which elaborate and secrete peroxidases, contain peroxidase activity in the same cell compartment (562, 957, 1114, 1296). Thus it may be assumed that sorne analogies exist between the intracellular route of peroxidases in animal and plant cells. This route 1eads to the exocytosis of peroxidases. In animaIs, several stimuli inducing this exocytosis are known, e.g., carbamylcholine in 1acrima1 glands (562), or calcium (1061).

In plants, too, severa1 factors causing peroxidase re1ease into the cel1 wall are known. These include osmotic shock (1480), ethy1ene (1109, 1110), and air pollution (Castillo, personal communication); whi1e gibberellins, for instance, reduce the re1ease of peroxidases (414). Peroxidase secretion in rat 1acrima1 glands was shown to be dependent on the presence of extracellular calcium, as is often the case for secretion processes (1061). Calcium was also recent1y shown to be invo1ved in the secretion of peroxidases by spinach cell suspensions (Sticher et al., 1981). In addition, it was reported that calcium has the property to bind sorne specific isoperoxidases to unidentified membranes in lenti1 roots (10 16) and in squash hypocoty1s (1024). This latter property cou1d be re1ated to peroxidase migration within the endomembrane system. Electron micrographs often show that peroxidase activity is closely associated to the membrane structure. The involvement ofcalcium in the control of the intracellular localization of peroxidase appears to be crucial, though much work is still necessary to understand it exactly. It therefore appears that calcium is likely to control peroxidase activity within the ceIl at several levels: viz, activation of preexisting enzyme molecules, fixation of sorne of these enzymes to selected membranes, and re1ease of the enzymes out of the cell by exocytosis.

85 LOCALIZATION AND BIOSYNTHESIS

Another line of evidence suggests that peroxidases are also present in vacuoles, often in great quantities (124, 486). It appears that the enzymes are associated with the tonoplast (467, 1420). Vacuole membranes are considered as end-products of the endomembrane system, arising either from the endoplasmic reticulum or from the Golgi apparatus (Morré and MoIlenhauer, 1976). It is thus tempting to speculate that peroxidases synthetized in the endoplasmic reticulum migrate towards the vacuole(s) bound to membrane elements (993). Another explanation of the massive presence of peroxidases within the vacuoles can be found in the autophagy process characteristic of plant vacuoles. By this phagocytosis process, vacuoles are able to engulf cytoplasmic constituents such as portions of the endoplasmic reticulum, ribosomes, Golgi vesic1es, etc. (Matile and Wiemken, 1976). Peroxidases could weIl be incorporated into vacuoles during this transfer of material from the cytoplasm.

REFERENCES


ABELES, ER.; LEATHER, G.R. 1971. Abscission: control of ceIlulase secretion by ethylene. PLANTA 97: 87-91.

ALVAREZ, M.R.; KING, 0.0. 1969. Peroxidase localization activity, and isozyme patterns in the developing seedlings of Vanda (Orchidaceae). AMER. J. BOT. 56: 180-186.

BASTIN M. 1968. Effect of wounding on the synthesis of phenols, phenoloxidase, and peroxidase in the tuber tissue of Jerusalem artichoke. CAN. J. BIOCHEM. 46: 1339-1343.

CASTILLO, EJ.; PENEL, c.; GASPAR, Th.; GREPPIN, H. 1981. Masquage et démasquage des isoperoxydases de Pelargonium. c.R. ACAD. Sc. PARIS 292: 259-262.


CZANINSKI, Y.; CATESSON, A.M. 1969. Localisation ultrastructurale d'activités peroxydasiques dans les tissus conducteurs végétaux au cours du cycle annuel. J. MICROSC. 8: 875-888.

DE JONG, D.W. 1967. An investigation on the role of plant peroxidases in cell wall development by the histochemical method. J. HISTOCHEM. CYTOCHEM. 15: 335-346.

GAHAGAN, H.E.; HOLM, R.E.; ABELES, F.B. 1968. Effect of ethylene on peroxidase activity. PHYSIOL. PLANT. 21: 1270-1279.

GAYLER, K.R.; GLASZIOU, K.T. 1968. Plant enzyme synthesis decay of messenger RNA for peroxidase in sugar-cane stem tissue. PHYTOCHEM. 7: 1247-1251.

GRAHAM, R.c.; KARNOWSKY, M.J. 1966. The early stages of absorption of horseradish peroxidase in the proximal tubules of mouse kidney. Ultrastructural cytochemistry by a new technique. J. HISTOCHEM. CYTOCHEM. 14: 291-302.

GRAHAM, R.c.; LUNDHOLM, V.; KARNOWSKY, M.J. 1965. Cytochemical demonstration of peroxidase activity with 3-amino9-ethylcarbazole. J. HISTOCHEM. CYTOCHEM. 13: 150-152.

JONES, J.; HULME, AC.; WOOLTORTON, L.S.c. 1965. The use of polyvinyl - pyrrolidone in the isolation of enzymes from apple fruits. PHYTOCHEM. 4: 659-676.

KANAZAWA, Y.; SHICHI, H.; URITANI, 1. 1965. Biosynthesis of peroxidases in sliced or black rot-infected sweet potato roots. AGR. BIOL. CHEM. 29: 840-847.

LAVEE, S.; GALSTON, AW. 1968. Hormonal control of peroxidase activity in cultured Pelargonium pith. AMER. J. BOT. 55: 890-893.

MATILE, P.; WIEMKEN, A 1976. Interactions between cytoplasm and vacuole. In 'TRANSPORT IN PLANTS III, INTRACELLULAR INTERACTIONS AND TRANSPORT PROCESSES'. Stocking, c.R.; Heber, U. (Eds.). Springer Verlag, Berlin - Heidelberg - New York, pp. 255-287.

MATSUSHITA, S.; IBUKI, F. 1960. Peroxidase activity found in the ribonucleoparticles from pea seedlings and rabbit liver. BIOCHIM. BIOPHYS. ACTA 40: 540-542.

MORRE, D.J.; MOLLENHAUER, H.H. 1976. Interactions among cytoplasm, endomembranes, and cell surfaces. In 'TRANSPORT IN PLANTS III. INTRACELLULAR INTERACTIONS AND TRANSPORT PROCESSES'. Stocking, c.R.; Heber, U. (Eds). Springer Verlag, Berlin - Heidelberg - New York, pp. 288-344.


PALADE, G.E. 1975. Intracellular aspects of the process of protein secretion. SCIENCE 189: 347-358.

PLENISCAR, M.; BONNER, W.D.; STOREY, B.T. 1967. Peroxidase associated with higher plant mitochondria. PLANT PHYSIOL. 42: 366-370.

POUX, M. 1969. Localisation d'activités enzymatiques dans les cellules du méristème radiculaire de Cucumis sativus L. Activité peroxydasique. J. MICROSCOPIE 8: 855-866.

SIEGEL,B.Z.; GALSTON, A.W. 1966. Biosynthesis of deuterated isoperoxidases in rye plants grown in O

2°. PROC. NATL.

ACAD. SCI. USA 56: 1040-1042. STEPHAN, O.; VAN HUYSTEE, R.B. 1981. Sorne aspects of

peroxidase synthesis by cultured peanut cells. Z. PFLANZENPHYSIOL. 10 1: 313-321.

STICHER, L.; PENEL, c.; GREPPIN, H. 1981. Calcium-requirement for the secretion of peroxidases by plant cell suspensions. J. CELL. SCI. 48: 345-353.

VAN DUIJN, P. 1955. An improved histochemical benzidine blue peroxidase method and a note of the composition of the blue reaction product. REC. TRAV. CHIM. 74: 771-778.

VAN FLEET, O.S. 1959. Analysis of the histochemical localization of peroxidase related to the differentiation of plant tissues. CAN. J. BOT. 37: 449-458.

CHAPTER 5

PHYSIOLOGICAL PROCESSES MEDIATED BY PEROXIDASES

Peroxidases have been implicated in and associated directly or indirectly with various physiological processes, including abscission, aging and senescence, apical dominance, cold tolerance, dormancy, fruit development and ripening, germination and early development, irritation, reaction and resistance against parasitism, sex expression, tuberization, etc. (see Subject lndex).

There are two major problems in trying to assign a particular role for peroxidases in these different physiological events. First there is a lack of genetically defined peroxidases in studies on growth and development. Scandalios (1158) reports that defined peroxidase systems, from a genetic point of view, are found in barley, maize and oats, but we are not aware of the use of such information in developmental studies. Second, by changing the conditions of the in vitro incubation medium, it is possible to catalyze all the reactions mentioned above by almost all types of peroxidases. Furthermore, there is relatively little information conceming the cellular localization of the different isozymes, the immediate environmental conditions for the manifestation of their activity, or the specifie participation of each of them (if not of sorne groups) in the physiological process being investigated.

Besides the possible but not specifie involvement of peroxidases in many reactions, it would seem that, on the basis of available evidence, isoperoxidases play four major roles in growth and development, through their control and/or participation in :


5.1. Auxin catabolism and consequently the endogenous free auxin level.

5.2. Lignin formation and cell wall biogenesis.

5.3. Defense mechanisms against pathogens.

5.4. Sorne respiratory processes.

The effects of light on peroxidases are examined in section 5.5.

5.1. AUXIN CATABOLISM

The involvement of peroxidase in general and of sorne more defined isoforrns in particular in the control of endogenous auxin level, and thus sorne physiological processes dependent on auxin, has come from different in vitro investigations, the validity of which were subsequently examined in vivo and/or in situ.

The most cornmon and direct evidence was the establishment of a correlation between total peroxidase activity of a non-fractionated extract, the capacity of the same to degrade IAA which is commonly called 'IAA-oxidase' activity, in few cases (816a) the rough analysis of the so-called endogenous auxin level (unfortunately measured through biotests only until very recently), and the development of the physiological phenomenon.

More indirect evidence has come from studies either on the effects of exogenously applied positive (Mn2+, monosubstituted phenolics) or negative (polyphenols) effectors of peroxidase as IAA-oxidase, or on the endogenous variation of sorne of these effectors in relation to the particular phase of the physiological phenomenon (Hare, 1964; Gaspar, 1965; Pilet and Gaspar, 1968). More refined correlations were established

91 PHYSIOLOGY

later after the fin ding by Mazza et al. (852) and Ricard and Job (lI 0 1) that the more basic (cathodic) were the isoperoxidases, the higher was their oxido-reduction potential against IAA and consequently their capacity to destroy IAA in vitro (at acidic pH, in the absence of added peroxides, thus essentially through their intermediary Compound III). In several auxin-dependent physiological and developmental studies there have been changes in fast moving cathodic isoperoxidases which have been indirectly or directly correlated with the endogenous auxin leveI. Below we give a few examples :

5.1.1. Cirovvth

In investigating maize dwarfism, Van Overkeek as far back as 1935 and 1938 showed that dwarf forms of this plant contained less auxin than normal ones and that their extracts destroyed the phytohormone at a higher rate. The higher peroxidase/IAA-oxidase activity ofdwarf types was confirmed later for different plants (Kamerbeek, 1956; Chrometzka, 1958; McCune and Galston, 1959; Pilet and Collet, 1960; Gorter, 1961; Evans and Alldridge, 1965; 987, 1248). It was shown for maize by Leyh et al. (1963) that this reduced activity of dwarf forms could be attributed to a higher amount of inhibitors of a phenolic nature (Bouillenne-Walrand et al., 1967).

Liang et al. (761) showed that a relationship existed between height genes and peroxidase. They measured specifie peroxidase activity from internode tissue of different height isogenic lines of sorghum. Tall plants had less peroxidase per gram tissue than their short counterparts; their FI offspring internodes were doser but had more peroxidase than the tal1 parent. Peroxidase in the Fo offspring was inversely related to their height and followed a sim ply inherited pattern similar to that for height. No such correlations were found between nitrate reductase or acid phosphatase activities and height in these isogenic tines. The authors conduded that peroxidase activity was not associated with height by chance and that it probably had a functional relationship. Similarly the association between plant height and peroxidase activity


was found highly significant and negative in seven varieties of bread wheat belonging to diverse genotypes, and their FI crosses (1230). The lesser peroxidase activity in taller wheat varieties would result in the accumulation or conservation of auxin which ultimately enhances the growth.

Palmieri et al. (987) found that homogenates of tomato tissues oxidized IAA at a rate proportional to their peroxidase activity. Two monogenic recessive mutations were involved in the control of this peroxidase activity. An inverse correlation was observed with two high peroxidase mutants and leaflet size (length and weight) and their epinastic and geotrophic-like behaviour. Enhancement of an organspecific fast-moving cathodic isoperoxidase was observed in these mutants.

Galston and Davies (1969) in discussing genetic, hormonal and environmental interactions in peroxidase/lAA oxidase activity presented evidence (mostly from in vitro cultured tobacco pith) to suggest that gibberellin, auxin, cytokinin and ethylene can interact to control the level of peroxidase in the tissue. The auxin-cytokinin interaction on growth has been shown to be correlated with their interaction on specific cathodic isoperoxidases (450) resulting in the endogenous auxin level control (Darimont et al., 1971). The spectacular growth effects of exogenously applied gibberellin have been shown to be preceded either by an increase in peroxidase/IAA oxidase polyphenolic inhibitors (Galston and Warburg, 1959; Leyh et al., 1963) or by a depressing effect on fast-moving cathodic isoperoxidases (1022, 1133). Gibberellic acid promotion of expansion of spinach cells was similarly correlated with a simultaneous suppression of peroxidase secretion in the culture medium (414). These findings explained the sudden increase in endogenous auxin after gibberellin treatements (Nitsch and Nitsch, 1959; Kuraishi and Muir, 1962; Gaspar and Bouillenne-Walrand, 1966). The gibberellin antagonistic effects of growth retardants like CCC can be interpreted through their inverse action on the same isoperoxidases (Lacoppe and Gaspar, 1968; Gaspar and Lacoppe, 1968; 428, 1133).

It must be mentioned that sorne data do not indicate any significant effect of GA on peroxidase activity or anycorrelation with the auxindestroying capacity of the tissues (879, 963) but these can be explained on technical grounds, as resulting from the molarity of the buffer used or the 'cell fractions analyzed (188). It was also found that CCC did not affect specifical1y the isoperoxidase spectrum of wheat seedlings,

93PHYSIOLOGY

but that microsomal-bound peroxidases were more abundant in extracts of CCC-treated plants, and that CCC .interacted with the Ca-mediated binding of peroxidases to membrane structures (133).

The inhibitory growth effects of light seem to depend also on the variation of the activity of sorne peroxidases. In etiolated pea stems the cofactor is kaempferol, which is present in low concentration. Illumination of plants by red light increases kaempferol synthesis in stems, which acts as a monosubstituted phenolic cofactor to increase peroxidase/IAA oxidase activity and consequently leads to a decline in stem growth (Mumford et al., 1961).

In cell suspension cultures of Phaseolus (38, 39) and of Si/ene (747, 748) cultured on 2,4-0, drastic changes were observed in the peroxidase zymograms during the growth cycle, i.e., total peroxidase and IAA-oxidase activities decreased in parallel during exponential growth and increased when growth rate was low. Old cells contained isoperoxidases, found previously in the nutrient medium. The selective release of isoperoxidases by young cells did not occur in senescent cells (747, 748). Cytochemical studies also showed that the enzymes were mainly cytoplasmic in young cells and mainly associated with the wall in older cells (38).

Oevelopment of peroxidase/IAA oxidase isozymes was also differentially associated with 2,4-0 growth promotion or inhibition in Nicotiana (736), Daucus (180, 1445), Trigonella (60), Beta vulgaris (Kevers et al., 1981a and b) and Arabidopsis (181, 938) callus tissues. In these latter cases, 2,4-0 affected fast moving cathodic isoperoxidases which once more indicates that it might act by altering the level of endogenous natural auxins. Our feeling, based on the literature (1218) and personal experimental data, is that most of the synthetic auxins modify growth and other 'auxin'-dependent physiological processes by this same mechanism.

The literature regarding the auxin dependence of so-called habituated tissues has been reviewed in recent years (134, 690, 1305). The idea that there is insufficient endogenous auxin for growth of normal auxinrequiring tissue in vitro was generally accepted although, due to technical problems, very few valid auxin measurements (Syono and Furuya, 1972; Nischio et al., 1976) have been made. The controversial suggestion that the rate of enzymatic inactivation of indoleacetic acid (lAA) is higher in auxin-requiring tissues received sorne support from more refined analyses of peroxidases (lAA-oxidase) isoenzymes and of their

94 PEROXIOASES 1970/1980

inhibitors, the so-called auxin-protectors (Stonier, 1970). However, such a parallel analysis of peroxidase isozymes, auxin content and auxin protectors had never been performed at the same time on auxin-requiring and auxin-nonrequiring tissues of the same plant untiJ recently (Kevers et al., 1981 a). A GC-ECO titration of IAA in normal auxin (2,4-0)requiring and auxin-independent (habituated) sugarbeet callus revealed an equal amount in both tissues. A comparison of the content and pattern (through starch gel electrophoresis) of soluble, membrane and wall peroxidases indicated that normal tissues contained a higher leve1' of isoperoxidases. Normal tissues were also found to contain higher levels of peroxidase inhibitors and auxin protectors (Kevers et al., 1981 a). The hypothesized peroxidase-mediated higher rate of auxin destruction in normal sugarbeet callus is supposed to be counterbalanced by the 2,4-0-controlled auxin protectors. The invoJvement of inhibitors of lAA-destruction in the process of induction for auxin-nonrequiring calluses was confirmed by Syono (1305) and 2,4-0 control of auxin protectors was further proved by Kevers (1981). Thus, an alternative way of action of the synthetic auxins is via a more indirect control of peroxidases through these auxin protectors, as has been shown to be the case for gibberellin.

Senescence generally occurs after the cessation of growth and inc1udes a series of processes leading to cell disorganization. Associated with cell membrane disintegration (Winkenbach and Matile, 1970; Matile and Winkenbach, 1971) and hydrolysis ofce]] wall polysaccharides (Wiemken-Gehring et al., 1974), there is an increase in respiration (see below). A plausible generalization of senescence (Mayak and Halevy, 1980) is that it corresponds to a higher oxidation state of the tissues, which may be in the form of accumulation of peroxides (Brennan and Frenkel, 1977) or in lipoxygenase activity, resulting in iipid hydroperoxides. This increase of peroxides and free radicals (Mishra et al., 1976) is apparently related to an increased activity of peroxidases in senescing petais at least (149; Carfatan and Oaussant, 1975; 1343). Indeed, treatment of flowers with free radical scavengers delayed senescence of carnation flowers (Baker et al., 1977). Gilbart and Sink (1971) assigned to auxin a central role in the control of senescence in poinsettia. The auxin level decreased in two poinsettia cultivars, but it decreased faster in the short-lived cultivar. Also, the activity of IAAoxidase and the level of hydrogen peroxide increased with aging.

95PHYSIOLOGY

The above-mentioned increases in peroxidases, peroxides and free radicals presumably were also involved in ethylene production (see Section 2.3.4; Beauchamp and Fridovitch, 1970). On the other hand, application of ethylene also enhances peroxidase activity (see Subject Index) and catalyzes the synthesis of ethylene by plant tissues. This phenomenon is corn mon to both jlower senescence (Mayak and Halevy, 19S0) and ripening of climateric fruits (1 136).

The function of increased peroxidase activity in fruit ripening has also been examined (see Subject Index). Haard (496) found peroxidase in both the soluble and residue fractions in pear, but the increase in activity occurred in the particulate enzyme, and this was associated with two isozymes not found in the soluble fraction. In this connection, Ku et al. (70S) reported that during tomato ripening the threefold increase in soluble peroxidase was associated with loss of one and formation of three new isozymes. They suggested that the enzyme might be involved in ethylene synthesis during ripening, although this view is disputed (653). During ripening of mangoes the c1imacteric and ethylene production were attended by a large increase in activity of peroxidase and catalase, which was associated with the disappearance of a heat-Iabile, non-dialyzable inhibitor of these enzymes (Mattoo and Modi, 1969). An increase in these enzymes was also induced by treatment of mango tissue slices with ethylene.

Auxin has been shown to retard ripening of banana (VendreII, 1969) and grape (Hale et al., 1970), and in the latter fruit endogenous auxin declined at the time that ripening commenced. Since peroxidase has the capacity for IAA breakdown, it couId provide a basis for control of ripening, i.e., by destroying endogenous IAA and thereby rendering the tissue sensitive to ethylene. Frenkel (399) investigated isozymes of peroxidase and IAA oxidase in pear, tomato, and the nonc1imacteric blueberry and found an increase in from one to three isozymes of IAA oxidase in each of the fruits during ripening, but he found an increase in peroxidase isozymes only in pear and tomato. He suggested that the increase in IAA oxidase in both c1imacteric and non-climacteric fruits was consistent with the view that fruit ripening is accompanied by an increase in capacity for auxin degradation, which is necessary to make the fruit sensitive to ethylene.

This view agreed with the reports that grape ripening was initiated by the disappearance of auxin (Coombe, 1960), and pear ripening was inhibited by infiltration with auxin (Frenkel and Dyck, 1973). A more

1""" "" \."


detailed study of peroxidase variation as a function of storage time for Golden Delicious apples (471) gave two peaks. The first peak corresponded to c1imacteric and was apparently associated with breakdown of hormones that retarded ripening. The second peak corresponded to the start of senescence and couId we11 be a defense mechanism against hydroperoxides. Peroxidase isoenzyme patterns were similar during the ripening and senescence stages (125).

If there is any causal relation between the rise in peroxidase activity and senescence, Birecka et al. (112) speculated that it might be mainly related to elimination of H

20

2 , whose production in ce11s increased

with senescence. This could be physiologica11y important since a decrease of catalase activity in senescing 1eaves has been often observed (e.g., Dhindsa et al., 1981). Thus, an increase in peroxidase activity wouId represent an induced protective action, perhaps delaying senescence.

When senescence indeed starts in 1eaves there is increase in the activity of peroxidase along with that of catalase (146, 221, 614). This elevation in peroxidase activity corresponded to an increase in anodic and cathodic peroxidases (167, 221, 659). Yellowing 1eaves with ethylene also showed increased peroxidase activity (294).

Peroxidase activity has also been linked with the abscission of leaves of cotton (894), bean (515, 1045, 1420), coleus (Sutcliffe et al., 1969), tobacco (543, 546, 550, 554), citrus (442) and fruit of cherry (1046, 1444). Both peroxidase activity and abscission are generally enhanced by ethylene (Addicott, 1970; Beyer and Morgan, 1970; 1). Part of this enhancement in enzyme activity could we11 be related to the decrease in auxin level which has long been known to occur prior to abscission in several systems (Addicott, 1970; Morgan and Durham, 1972; 442). Lignification through acidic peroxidases couId protect the exposed scar (Addicott, 1970). The close correlation between the increase in peroxidase activity and cell wall weakening may also suggest an association with changes in hydroxyproline-rich proteins, which in tum affect the extensibility characteristics of the walls, as mentioned by Lamport (725) and Ridge and Osborne (1109, 1110).

97 PHYSIOLOGY

5.1.2. Morpho- and ûrganogenetic Processes

The so-called thigmomorphogenetic process (Jaffe, 1973) is essentially a growth perturbation due to a mechanical stimulus. Rubbing young intemodes of Bryonia dioica, which significantly decreased their elongation, was followed by rapid changes in soluble and ionicallybound cell wall basic (cathodic) peroxidases, and with the appearance of an additional isozyme (144). A decrease in the IAA level (quantified by a GLC-ECD technique) in the intemodes was correlatively shown (Hofinger et al., 1979). Pretreatment of the Bryonia plants with lithium prevented the peroxidase changes (namely the appearance of the specific isoperoxidase characteristic of rubbed plants) and the inhibition of elongation due to rubbing (140). A similar relationship between a rapid increase of activity of basic peroxidases and a mechanically induced (by pricking) growth inhibition has been shown in Bidens pilosus plants (Desbiez et al., 1981).

The dependence of the rooting and flowering processes on auxin, if not their obligatory requirement for critical auxin levels, has been discussed for a long time, but without any precise concepts until recently. Absence of suitable· techniques for IAA identification and quantitation as weil as the absence of suitable biochemical markers played important roles in the lack of precision. An intensive comparative study of both processes using peroxidases of different plant materials has considerably c1arified the apparently divergent situations (Gaspar, 1981; 444, 445) as indicated schematically in Figure 14.

An induction phase in the rooting process (in which no histological events are observable) is characterized by a rise of the total peroxidase activity of the whole cutting. Root primordia initiation takes place following the peak ofactivity during a decrease of the basic isoperoxidases. Flowering is associated with inverse variations of total enzyme activity and basic isoperoxidases in inductive and initiative phases. Explants, which have reached the rooting or flowering inductive phase on the mother-plants can directly initiate root or flower primordia when cultured in vitro. Considering that basic isoperoxidases are responsible for the in vivo auxin catabolism, it has been hypothesized that rooting and flowering are controlled by inverse variations of the auxin level in their inductive as weil as their initiative phases (Fig. 14). Auxin analyses and available literature data have supported this view (Gaspar, 198\). The following examples illustrate the working of this scheme.

• • • •

98 PEROXlDASES 1970/1980

Spinach is a long day plant, which does not f10wer in short days. However, after growth under short days for 1 month, f10wering is rapidly induced in less than 24 hr, by transfer to long days or to continuous light. lt can also be induced to f10wer under short days by the application of GAl (Penel, 1976). Transfer to long days or treatment with GA) leads to rapid dec1ine in cathodic peroxidases and

. ROOTING FLOWERING

PRE - INDUCED EX PLANTS

® 1 1

o 1 acidic p. /'1 basic p.1 \. 1

1

NON -INDUCED EXPLANTs

acidic p. /' acidic p. )' acidic p. ~ 1 acidic p. ~ basic p. /' basic p. \. basic p. / _~ basic p. /

/ " l ",1 1 l '

1 / 11 1 1

1 1 ® " i @1 1 1 1 1 1

1

1 1 1" 1

1 1

11

1 '" --.J1__ / / 1

1

1 DAYs

INDUCTION INITIATION INDUCTION INITIATION

© ]::.:;:

acidic p. /' 1 11 basic p. .J'

~/ DAYs

Qi <Il Cl "0

X o .... Qi Cl.

Ci ;§

c X :::J Cl

<Il :::J o C Qi 01 o "0 C

W 1 1 1

Fif(. 14. Schematic representation of vanatIons in peroxidase (p.) and auxin levels during the course of the inductive and initiative phases of rooting and nowering by preinduced and non-induced explants (afier Gaspar, 1981).

99 PHYSIOLOGY

an increase in anodic peroxidases. After 48 hours there is a progressive increase in cathodic peroxidases. Similarly during flower formation in vitro in tobacco epidermal explants, there is a continuous increase in fast moving cathodic isoperoxidases (1328). But this comparison could only be made after having defined histologically that the transition of the spinach meristem from the vegetative to the floral stage (479) was taking place, and after having biochemically characterized tobacco plants in their vegetative and the floral states, with respect to gradients along their stem and floral axes (1328). Induction of flowering and of other phytochrome-dependent processes could be obtained through photomodulation and photodetermination of the same types of peroxidases (1020, 1174, 1175).

During rooting of stem tips of Prunus (1063), of adventitious shoots in Asparagus (1375), and of epidermal explants of tobacco (448, 1328) there is an increase in intensity of fast moving cathodic peroxidases up to a maximum. This is fol1owed by a decrease in intensity, ail prior to the morphological appearance of the roots. Knowing the histology of these processes, Gaspar et al. (446) proposed that root initiation involved at least two phases, viz: an induction phase in which no histological events are observable, followed by an initiative phase in which root primordium formation begins. These two phases are marked with increased and then reduced peroxidasic activity and a reverse relationship in auxin content, i.e., a decrease in endogenous auxin fol1owed by an increase. This hypothesis can explain why phenolic compounds such as ferulic and chlorogenic will inhibit rooting if applied during the induction phase, and stimulate it during the initiation phase as shown by Smith and Thorpe (1977). Compounds such as these have been shown to interact with IAA oxidase and reduce the rate of IAA oxidation (see Gaspar et al., 1964; Pilet and Gaspar, 1968). Recently Lee (740) has shown that the phenolic inhibitors interfere with the first stage of IAA oxidation by preventing the IAA

. induced changes in the soret band of peroxidase. Apparently the peroxidase is prevented from reacting with IAA to form the highly reactive enzyme intermediates which lead to IAA degradation.

Variations in peroxidase and auxin levels during the course of de novo vegetative bud formation appear to be different from the above (Gaspar, 1981). De novo vegetative bud formation always occurs after a prior increase of peroxidase activity in the expIant (Kevers et al., 1981b; 448,569,745,750,800,806,927,938, 1131, 1327, 1328).


Acidic as weIl as basic isoenzymes are involved. The curve drawn from the results obtained with bud-forming epidermal layers of tobacco (448, 1328) has been found to typically give the same lag and plateau phases in the peroxidase activity evolution during bud formation as has been observed in other materials such as chicory leaf explants (745, 750), different tobacco systems including callus (800, 806, 1321, 1327), Arabidopsis (938) and sugarbeet (Kevers et al., 1981b). The apparently obligatory tempory maintenance of the plateau before bud

,-" .. initi~tion appears specifically related to this organogenetic process.

IAA levels have been compared in different subcultures of organogenetic and non-organogenetic habituated sugarbeet callus lines (Kevers et al., 1981 b) during the exponential phase of growth. Results indicated an average amount (+ or - 200 ng/g fresh weight) of the organogenetic callus six times less than that (+ or - 1200 nglg fresh weight) of the non-organogenetic one. Also an inverse relationship between these IAA levels and the corresponding soluble peroxidase activity (3.98 and 0.73 repectively) was obtained. This presumably leads' to an auxin-cytokinin ratio suitable for the induction of shoot formation (Skoog and Miller, 1975).

Similar indirect correlations between the peroxidase content, the endogenous auxin level and embryogenesis in habituated shamouti orange callus have been made. Embryogenic potential in ovular callus is associated with a notably higher peroxidase activity and with the appearance of an additional specific cathodic band (690). The same dark-grown embryogenic callus was shown to decompose IAA at a faster rate than non-embryogenic caHus (360). The embryogenic lines could also deactivate IAA by conjugating it with aspartate faster than non-embryogenic lines (1252).

Instead of considering the peroxidase mediation of physiological processes through auxin catabolism by the simple auxin disappearance two other explanations have been proposed and debated without final conclusion at the moment (Skytt Andersen et al., 1972; Roberts, 1974; 372, 373). One concept is that the oxidation of IAA catalyzed by peroxidase in plants yields products that stimulate growth (Tuli and Moyed, 1969; Basu and Tuli, 1972; Frenkel et al., 1975; 870). Another one considers the peroxidase auxin-oxidase complex as a system generating inhibitory substances among which methyleneoxindole would play the major role (Tuli and Moyed, 1967; Hofinger et al., 1980; 432, 438, 583).

PHYSIOLOGY 101

5.2. LIGNIN FORMATION

5.2.1. Growth

Fry's work (414, 415) has suggested that peroxidase restricted cell extension and expansion by making the cell wall rigid in two ways :

a) covalently by catalyzing the conversion of feruloyl side-chains into diferuloyl cross-links and

b) non-covalently by catalyzing the conversion of soluble phenolics into hydrophobic quinones (or polymers).

GA3

is hypothesized to prevent this process by inhibiting peroxidase secretion (414).

Lignification is considered to be executed more specifically by the involvement of acidic peroxidases (Nakamura and Nozu, 1967; 1445, 1447). It is quite interesting to note that this phenomenon seems to take place immediately after breakdown of auxins, mediated by the basic peroxidases. As an example, enhancement of anodic peroxidases in rubbed young intemodes of Bryonia (144) occurred progressively after variations of the cathodic ones. Old and already lignified intemodes, which do not grow anymore, are characterized by high activity of these same anodic peroxidases and they do not react to the mechanical stimulus.

Similarly, the cessation of elongation in Pisum sativum stems (424) and growth reduction in camation plants after infection (Pugin et al., 1979) had been attributed to a series of factors including peroxidase mediated auxin-destruction, peroxidase-induced lignification and extension-induced wall stiffening. These findings are probably related to the parallel ethylene-mediated increase of wall hydroxyproline level and activity of covalently-bound acid peroxidases (1109). Furthermore, it has been shown that soluble (Shannon et al., 1966; 904) and at least one of the three acidic covalently cell wall-bound peroxidases (283) contained hydroxyproline.

These results are consistent with the often done observation that the activity of ail types of peroxidases increases basipetally along with growth cessating and lignifying intemodes (Macnicol, 1966; Mills and Crowden, 1968; 144,425, 1328, 1375).


Very interesting in this respect are the results of studies of Marigo .(1979), who showed that tomato stem growth inhibition after root feeding with lignin-precursors resulted from an increase in the lignincellulose ratio subsequent to a rise in the activity in the cell wallbound peroxidases.

5.2.2. Differentiation - Vascularization

Usually, at the passage of the cells from a state of division to elongation and, particularly, to differentiation, the total peroxidase activity rises considerably. An investigation of four mutant genotypes of Pisum sativum has shown an inverse relationship between peroxidase activity and lignification of the pod membrane (138). From their developmental studies, the authors suggested that peroxidase predisposed cells to the lignification process per se : thus, cells in localized regions wherein lignification subsequently occurred, i.e. those cells which had become noticeably elongated, had a more intense peroxidase-staining reaction than did the neighbouring non-differentiating cells.

The increase in peroxidase activity in cells from the pea epicotyledon, which have ended their growth, would be due to an enhanced activity of sorne of the present isozymes rather than to the appearance of new ones (424). However, Sahulka (1141) found a peroxidase band in cells from the zone of differentiation in a root of broad beans which is not to be found in the zones of division and elongation. Upon the passage of the cells from a state of division and elongation and differentiation in germinating maize seeds,the increase of peroxidase activity is due both to the appearance of new enzymes (mainly cathodic) and the activation of som~e of the preexisting (namely anodic) isoenzymes (311).

That differe t isoperoxidases are associated with different types of cell differentiatio , mostly through lignification, has been confirmed by established corlrelations between a marked increase in enzyme activity and the lignification of the seed integuments of Encyclia (Alvarez, 1968), vascularization (264, 488, 525, 564, 1453), and fiber formation (499). Suberin contains a significant fraction of lignaceous materials.

103 PHYSIOLOGY

A high correlation between peroxidase activity and suberization was observed. Peroxidase content of suberizing cel1s (after wounding in potato) was more than 10 times higher than that of the immediately adjacent dividing cells (127, 129).

The appearance ofnew peroxidase isozymes in peanut cell suspension cultures was related to the cellular differentiation (1404). Varietal and seasonal differences in lignification of pear sclereids are also dependent on the association of peroxidase with cell walls (1074).

It has also been suggested that the continuous increase in activity and number of fast moving anodic peroxidases in the course of root, bud and flower formation was associated with a continued lignification process for xylem cells differentiation in these newly formed organs (445, 1328).

Contrary to lignification in aging tissues which seemed to be preceded if not correlated with a decrease in the endogenous auxin level, lignification in differentiating tissues couId be induced by increased endogenous levels of IAA in these growing tissues. Differentiation indeed was shown to be associated with the suppression of specifie isoperoxidases working as IAA-oxidases (181,736,938,1113,1445).

5.3. DEFENSE MECHANISMS AGAINST PATHOGENS

Plants are able to provide active defense against pathogenic organisms. Either, they are resistant, i.e., they prevent or restrict the infection, or they are susceptible,i.e., infection develops, inducing host damage. Peroxidases have been implicated in these two processes (Farkas and Kiraly, 1958; Kosuge, (969). Stahmann and Demorest (1264, 1265) reported that in plants inoculated with selected viruses, bacteria or fungi, there was a rapid increase in peroxidase and often the appearance of new peroxidase isozymes. Sorne isozymes disappeared


and new isozymes not seen in healthy plants appeared after pathogen infection. Changes in isoperoxidase pattern following inoculation has often been reported (483, 484, 1371). They may only affect one kind of peroxidase (for example ionically-bound peroxidase). Reports showing no changes in isoperoxidases are also available (1094).

Use of susceptible and resistant strains of cultivars generally have shown that the latter immediately reacted to inoculation of an infectious agent by an increase of peroxidase activity, while the former did not exhibit this increase (1401) or reacted with delay to inoculation (1094). Generally, resistant plants had a greater peroxidase activity than susceptible plants before inoculation (1365). Beside natural resistance to infection, resistance may be induced by a first infection or by a chemical or physical agent. This acquired resistance was often correlated with an increase of peroxidase activity. It has been reported to be induced in tobacco Ieaves by prior injection of heat-killed cells of Pseudomonas tabaci. Recently, Venere (1401) found no effect on peroxidases when heat-killed Xanthomonas were injected to cotton cotyledons, while living bacteria induced a strong increase.

Among the chemicals inducing peroxidase increase and resistance development, ethylene is one of the most effective. Increased peroxidase activity and resistance to black rot was found in sweet potato roots incubated above infected roots in closed containers (Clare et al., 1966). Apples, a source of ethylene, may replace infected roots in inducing resistance. Ethephon, an ethylene precursor, also increased both the resistance of susceptible tomato plants to Fusarium and their peroxidase activity (1094). Ethylene, which could induce the release of peroxidases by plant cells is known to be an element in the defense mechanism (Paradies and Eistner, 1980). In tobacco leaves infected with tobacco mosaic virus, a gradient of enhanced peroxidase activity from the lesion edge to the tissue between the lesions was found (1430). In addition to this localized reaction, several authors have observed the development of a systemic induced resistance. This means that lesion formation in lower Ieaves was followed by the appearance of resistance in upper Ieaves, although the virus remained confined to the necrotic area. Peroxidase activity increased in parallel with the development of resistance of non-infected leaves (1121,1122, 1394, 1395). There is therefore a large body of reports showing the positive correlation between high peroxidase activity and resistance to pathogens (see also Subject Index).

105PHYSIOLOGY

Several functions may be attributed to peroxidases in relation to the mechanisms of defense against infection. Lignification of diseased tissue may be a mechanism of resistance (Vance et al., 1980). As peroxidases are involved in lignin biosynthesis (see Section 2.3.3), the increased peroxidase activity following pathogen inoculation may intensify the formation of lignin. This hypothesis was confirmed by Vance and coworkers (13 70, 13 71) who showed that cycloheximide, which inhibited the resistance of canarygrass to Helminthosporium averae, also blocked lignin biosynthesis and activity of enzymes involved in lignin formation, including peroxidases. New formation of lignin could prevent the penetration of the pathogen.

An alternative role of peroxidases in the resistance to viruses was proposed by Simons and Ross (1122). They proposed that these enzymes kill the infected cells, thus suppressing the multiplication of the virus. However, it seems reasonable to think. that peroxidases are mainly used by plants to attack pathogens. Two different mechanisms have been proposed. The first one involved the production of oxidized phenols arising by the action of wall peroxidases and phenoloxidase (Kojima, 1931; 1366). Venere (1401) recently demonstrated that peroxidase isolated from blight-resistant cotyledons formed a product, which was bactericidal to Xanthomonas malvacearum, when incubated in the presence of catechin and hydrogen peroxide. The production of these two compounds was enhanced during infection. Peroxidases also killed bacteria or fungi by another mechanism which was extensively studied in animal systems. The myeloperoxidase or lactoperoxidasehydrogen peroxide-halide system is known to have a strong antimicrobial effect (Jago and Morrison, 1962; Klebanoff, 1967; 634, 100 1). The white blood cells are able upon activation to produce all the elements of this system, including hydrogenperoxide. It is tempting to draw a parallel between plants and animaIs regarding the antimicrobial function of peroxidases. Lehrer (1969) demonstrated that in the presence of hydrogen peroxide and potassium iodide, human myeloperoxidase and horseradish peroxidase were rapidly lethal for several species of fungi. Southern bean mosaic virus was also irreversibly inactivated by exposure to horseradish peroxidase, potassium iodide and hydrogen peroxide (1366a). In addition, there is indication that during host-parasite interactions, hydrogen peroxide production was enhanced (98 la). This production of hydrogen peroxide is dependent on wall peroxidase (see Section 2.3.3). The incorporation of iodide in organic compounds in plants has also been established (André, 1973). Thus, the possibility


exists that plants use the iodide-hydrogen peroxidase system to kill parasites. Several phenols enhance the bactericidal effect of this system (1366).

Despite ail the positive correlations existing between peroxidases and plant resistance to pathogens, many authors have concluded that peroxidases do not play an active role in the mechanism of defense against infection. This conclusion is often based on the observation that enhanced peroxidase does not always coincide with resistance. For example, when inoculated with Puccinia graminis tritici, leaves of resistant wheat kept at 20°C exhibited an increase of peroxidase activity. After transfer of this resistant plant with increased peroxidase activity to 26°C, reversion to a susceptible infection type occurred, but peroxidase activity did not decrease during the reversion process (1180). Treatment of susceptible lines of wheat with ethylene induced an increase of peroxidase activity to levels above the activity exhibited by resistant leaves, but treated leaves remained susceptible (271 a).

In tobacco, injection of leaves with sorne polyanions induced resistance to mosaic virus and an increase of peroxidase activity, but the two phenomena apparently were not related (1267). Increased peroxidase activity was also observed in tobacco leaves infiltrated with heat-killed bacteria, but this treatment only induced disease resistance in leaves which were not kept in darkness. Similarly, increased peroxidase activity was observed after treatment which did not induce resistance. Nadolny and Sequeira (921) concluded from these data that the peroxidase increase apparently parallels the development of disease resistance and that peroxidases were not directly involved in protection.

Several points however are never discussed in papers concerning l,,;'

the relation between peroxidases and the mechanisms of plant defense :

1) plants may react to pathogens by a release of peroxidases from cells into intercellular spaces, without change in the total measurable activity of the tissue;

2) the enzyme is one element of the peroxidase system and is only active when hydrogen peroxide and phenols (catechin for example) or halide is available.

These two facts could explain why resistance and increased peroxidase activity are not always correlated. However, it is clear that plant peroxidases certainly have bactericidal and fungicidal properties.

PHYSIOLOGY 107

5.4. RESPIRATION

In addition to the components of the tricarboxylic acid cycle, the cytochrome and oxidative phosphorylation system, mitochondria probably contain certain other oxidative enzymes (Nicholls, 1965; Aylward and Haisman, 1969). Mitochondria from both animal (Neuberg et al., 1962) and plant (Hackett and Ragland, 1962; Ivanova et al., 1966) sources do indeed possess peroxidase activity which can be resolved into a variable number of isoenzymes (279, 434). Rubin and Ivanova (1963) showed that peroxidase can provide an alternate route for oxidation of reduced nicotinamide adenine dinucleotide and it was suggested (362) that one or more such mitochondrial peroxidases may constitute a secondary pathway for electron transport without coupling at the third site of oxidative phosphorylation. Further investigations (1103) have revealed the presence of significant levels of peroxidase and hydrogen donor to peroxidase in gradient-purified mitochondria from mung bean hypocotyls. These could easily utilize any hydrogen peroxide produced by the alternate oxidase pathway. Similar experiments performed upon submitochondrial particles demonstrated a rate of H101 production which could easily account for the net electron flux through the alternate pathway. It is postulated (1103) that the alternate pathway reduces oxygen partially to hydrogen peroxide, and that the peroxidase (and catalase) activities of the mitochondria prevent its accumulation.

A strong correlation has been shown to exist between peroxidase activity and respiration rate during germination of rice. This finding has led to peroxidase being considered as part of the respiratory mechanism of the seedlings (999). It has also been observed in many plants that peroxidase activity and respiration rate invariably increase in parallel following infection (Rubin and Ivanova, 1958; 1390).

Several investigations have demonstrated that peroxidase activity increased, with changes in its pattern, with the climacteric rise of fruits (see 500). This has implicated peroxidase in the control of respiration. Particulate peroxidase levels increase 3-fold with the initiation of the respiration climacteric (496). However, these variations might be due to differential phenol inhibition (500).


5.5. LIGHT MEDIATED PROCESSES

5.5.1. Peroxidases as pigments

Peroxidases may be considered as pigments since they absorb visible light. The question which naturally arises concerns the possibility that light modifies the catalytic functions of peroxidases or even acts on the physiology ofplants, in part, through its absorption by peroxidases. No definite conclusion one way or the other can be drawn from the literature. There have been many reports on the photochemistry of hemoproteins; e.g., flash photolysis has been used to measure the photodissociation of carbon monoxide complexes of hemoprotein (Hasinoff, 1974). In addition, complexes of peroxidases with cyanide were also found to be photosensitive (Keilin and Hartree, 1955). More recent reports of Stillmann and coworkers (1275, 1276) have shown that low energy polychromatic light of wavelengths between 320 and 450 nm can catalyze the conversion of HRP Compound 1 to Compound II and Compound II to ferriperoxidase. These reactions occurred at room temperature.

Earlier Sano (1147) had shown that upon aerobic oxidation of IAA, HRP was converted to a verdotype substance having absorption maxima at 405, 530 and 670 nm. This substance, designated P670, when kept in darkness, was gradually converted into another substance having absorption maxima at 403, 530 and 630 nm (P630). P630 was reversibly returned to P670 upon light irradiation. Evidence indicated that P630 and P670 had the same chromophore, a formylbiliverdine. P630 was shown to be a complex containing carbon monoxide, dissociable by light to yield P670. The author found that only specific isoperoxidases were transformed into P670 and that P670-like compounds were present in living tissues. The possible physiological significance of these compounds remains to be elucidated.

109 PHYSIOLOGY

5.5.2. Peroxidases and phytochrome

A large number of enzyme activities are dramatically changed during the de-etiolation of dark-grown seedlings (1175). This effect of light is mediated by the chromoprotein, phytochrome. Phytochrome exists under two forms with different absorption spectra. Etiolated darkgrown seedlings only contained P, the form having its maximum

- r absorption at 660 nm. Vpon irradiation, up to 80 per cent of the phytochrome molecules were converted to Prr , the form having its maximum absorption at 730 nm. P the so-called active form ofrr, phytochrome, is responsible for the changes observed in enzymatic activity. Red light, which increases Prr percentage has physiological effects opposite to far-red light, which decreases Pre Operationally, an enzyme regulated by phytochrome should react in an opposite way to red and to far-red light (1175).

The regulation of peroxidase by phytochrome was described by several authors (Mohr, 1972; 1175, 1237). Light often induces an increase of peroxidase activity in etiolated seedlings. This was reported in mustard cotyledons (1176), maize leaves (1194), bean hypocoty1 hook (292) and root and cotyledons of radish (592). The development of extractable peroxidase activity in the mustard seedling was controlled by phytochrome in an organ specific manner, i.e., enhancement in the cotyledon and taproot, inhibition in the hypocotyl (1 I76). The same specificity was observed in radish seedlings (592). Schopfer (l174a, 1175) made a distinction between modulation and determination as modes of regulation in phytochrome-mediated photomorphogenesis. In mustard cotyledon the response of peroxidases to light involved two steps. In the first one, the response was induced by Prr while in the second one the increase of peroxidase activity occurred. Schopfer suggested that in the first light requiring step, inactive peroxidases were synthetized and that in the second step these inactive enzymes became activated by a process not involving PI;-. In contrast, the peroxidase activity in etiolated maize leaves was photomodulated (1194). This means that peroxidase activity increased as long as P,Ir was present. In a series of papers Sharma and coworkers have reported that (i) the regulation of peroxidase activity by phytochrome did not involve the participation of kinetin, gibberellin, acetylcholine or c-AMP (1195), (ii) that there was an age dependence of the phytochrome regulation of peroxidase which mainly affected the 'soluble peroxidase' (1196), (iii) that photosynthesis was not involved in this regulation (1197).


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PHYSIOLOGY 111

As far as light-grown green plants are concerned little is known about the possible relation existing between phytochrome and peroxidases.

-Actually, the physiology of phytochrome in non-etiolated plants is not yet fully investigated. A peroxidase with, a basic isoelectric point, extracted at high pH from spinach was shown to rapidly react to short irradiations with red or far-red light (1019,1020). This peroxidase activity underwent a fluctuation after an irradiation of 1 or 2 min (Fig. 15a) and the shape of the fluctuations was dependent on the light quality. An interesting fact concerning this effect was that the photoconversion of phytochrome in sorne leaves of the plant immediately modified the peroxidase activity in other leaves (Fig. 15b; 1021, 1026). This implied the fast transmission of sorne signal from leaves to leaves which was triggered by phytochrome photoconversion. This transmission was inhibited by several substances including lithium chloride, EGTA and the Ca2+ ionophore A23187 (Karege et al., 1982). Figure 16 shows a mode! which accounted for the experimental data (1026) : the transmission of the signal generated by phytochrome would result from changes in K+ distribution; K+ changes would be correlated with modification of cellular Ca2+ which itself controis peroxidase activity distribution and/or synthesis within the cells. Red and far-red light was also reported to affect peroxidase pelletability in extracts from spinach leaves. This is possibly due to a different association of peroxidases to the plasmalemma (1023). An effect of phytochrome conversion in vitro was also demonstrated in membrane suspensions of Cucurbita pepo (1025). ln that case, red and far-red light pulses changed the peroxidase activity associated to membranes in an opposite way.

The quality of light under which plants are grown seems to have a great influence on peroxidase activity. In tomato leaves infected with Septoria lycopersici peroxidase activity was greater under green and red light and lower under orange and blue light (92, 93). ln spinach leaves, peroxidase activity was greater under blue light than under red light (Penel, 1976). In this latter case, no qualitative differences in the isoperoxidase patterns were observed between blue- and red-light grown spinach. The difference in total activity was due to cationic peroxidases which were more active under blue light. Disks from leaves grown under blue light also destroyed IAA more effectively than disks from leaves grown under red light. This observation is in agreement with the fact that spinach leaves are smaller under blue light.


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Finally, germicidal ultraviolet light enhances peroxidase actlVlty in detached bean leaves, inducing the appearance of two isoperoxidases. The effect of uv is partially reversed by near-uv (SOl).

5.5.3. Photoperiodic control and flowering

The relative length of the day and night is a major element in the determination of plant growth and development. Therefore, it can be expected that peroxidases would be affected by photoperiod. Unfortunately, there are only a few published studies on this aspect of the regulation of peroxidases by light. Warner and Upadhya (1968) showed that the shoot tips of Clementine tangerine and of trifoliate

113PHYSIOLOGY

orange had higher peroxidase activity when grown under long days as compared with short day-grown seedlings. In tobacco leaves, a group of isoperoxidases which migrate slowly toward the anode was found to become less active with increased day lengths (295). These two reports appear to be contradictory. However, Parish (1969) has shown that in wheat, light decreased the specific activity of peroxidase in leaves and increased it in coleoptiles. One could reasonably expect that light wouId have different effects on different organs, as it has opposite effects on the growth rate.

A study with Cichorium leaf tissues showed that tissues cultured in darkness have a greater peroxidase activity than those cultured under light. Transfer of tissues from darkness to light induced a decreased activity and vice-versa. Phenolics in light- and dark-grown leaves were distributed in an inverse manner. This study leads to the conclusion that peroxidase activity could be controlled by phenolic compounds which primarily respond to light (746, 749). That phenolics vary qualitatively and quantitatively on exposure to light is a well-established fact (e.g., Engelsma, 1969). As an example, the oxidation of IAA by peroxidases from Pharbitis cotyledons is strongly affected by the presence of phenolic inhibitors. These inhibitors change according to the light conditions and could be responsible for the differences in enzyme activity observed (Konishi and Galston, 1964).

Peroxidase activity was extensively studied in relation to photoperiod and floral induction in spinach, a long-day plant. As far as total peroxidase activity is concemed, it appeared that young and old leaves react differently to photoperiod. In young leaves, peroxidase activity was stronger at the beginning of the short day than at the end, whereas in old leaves the activity was stronger at the end (Penel, 1976).

In addition, the peroxidase activity followed a characteristic timecourse during the life of the plant, reaching a minimum at the time when spinach becomes induced to flower (658) (see also Section 5.1.2). The floral induction was also characterized by a change in the balance between acidic and basic isoperoxidases (1022). Particular attention was paid to the basic isoperoxidases which responded rapidly to phytochrome photoconversion, as mentioned earlier. The shape of the fluctuation of this peroxidase activity, following a 2-minute irradiation with red or far-red light, was different in vegetative or in induced spinach leaves (660, 10 19, 1020). This difference could be used as a quick test to discriminate induced from non-induced leaves, as the


differences appeared weB before the onset of floral differentiation in the shoot apex. The transition from the shape characteristic of noninduced spinach to the induced one occurred soon after the end of the critical photoperiod, namely after 14 hours of light (660, 661). Several physical or chemical factors which promoted or delayed floral induction could be studied by using this peroxidase response as an indicator (Karege, 1981).

In summary, it is therefore possible to explain many physiological processes in the plant by involving specifie classes of peroxidases in functions in which they have clearly been shown to be capable of in vitro, and in many cases in vivo as weil. This role of peroxidases could represent course control ofgrowth and development, in which peroxidases respond to and interact with other factors such as phytohormones and metabolites as a consequence of any perturbation in the environment.

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PHYSIOLOGY 121

SMITH, D.R.; THORPE, T.A 1977. Root initiation in cuttings of Pinus radiata seedlings : efTects of aromatic amino acids and simple phenylpropanoids. BOT. GAZ. 138: 434-437.

STONIER, T. 1970. The role of auxin protectors in autonomous growth. In 'LES CULTURES DE TISSUS DE PLANTES'. Colloque int. CNRS, Strasbourg, pp. 423-435.

SUTCLIFFE, J.F.; ARCH, P.O.; LEGETT, P.A.; PHILLIPS, 8.J.; SEXTON, R. 1969. Enzymic changes occurring during the deveIopment of the abscission zone of Coleus blumei. Abstracts. XIth Internat. Bot. Congress Seattle, U.S.A, 213.

SYONO, K.; FURUYA, T. 1972. EfTects of cytokinins on the auxin requirement and auxin content of tobacco calluses. PLANT CELL PHYSIOL. 13: 843-856.

TULI, V.; MOYED, H.S. 1967. Inhibitory oxidation products of indole-3-acetic acid :. 3 hydroxymethyloxindole and 3methyleneoxindole as plant metabolites. PLANT PHYSIOL. 42: 425-430.

TULI, V.; MOYED, H.S. 1969. The role of 3-methyleneoxindole in auxin action. J. BIOL. CHEM. 244: 4916-4920.

VANCE, c.P.; KIRK, T.K.; SHERWOOD, R.T. 1980. Lignification as a mechanism of disease resistance. ANN. REY. PHYTOPATHOL. 18: 259-288.

VAN OVERBEEK, J. 1935. The growth hormone and the dwarf type of growth in corn. PROC. NAT. ACAD. Sc. (USA) 21: 292-299.

VENDRELL, M. 1969. Reversion of senescence : efTects of 2,4dichlorophenoxyacetic acid and indoleacetic acid on respiration, ethylene production, and ripening ofbanana fruit slices. AUST. J. BIOL. SCI. 22: 601-610.

WARNER, R.M.; UPADHYA, M.D. 1968. EfTect of photoperiod on isozyme composition of Citrus and Poncirus. PHYSIOL. PLANT. 21: 941-948.

WIEMKEN-GEHRING, Y.; WIEMKEN, A; MATILE, P. 1974. Mobilization von ZellwandstofTen in der welkenden Bluten von lpomoea tricolor (Cav.). PLANTA 115: 297-307.

WINKENBACH, F.; MATILE, P. 1970. Evidence for de novo synthesis of an invertase inhibitor protein in senescing petaIs of lpomoea. Z. PFLANZENPHYSIOL. 63: 292-295.

CHAPTER 6 L"· .

PRACTICAL APPLICATIONS OF PEROXIDASES

Since the paper of Peirce and Brewbaker (1010), reviewing the applications of the analysis of isoforrns of difTerent enzyme systems, proposais for the practical use of peroxidase as indicator of plant status have increased.

Peroxidase electrophoresis is an efficient tool for large - scale genetic investigations (1145) such as : identifying ramets, populations or species hybrids, deterrnining the efTect of inbreeding and pollen migration on the genetic structure of population and seed orchards; or aiding breeding programs through indirect selection or through development of breeding procedures.

Peroxidase electrophoresis has been proposed as an aid to identification and phylogenetic studies of oat varieties or cultivars (22, 1226, 1469, 1470), Datura species (241), peanut cultivars (211), flax genotypes and genotrophs (Tyson, 1969; 384, 385, 1353-1357), Nicotiana species (Trinh et al., 1981; 574,1081,1201), Petunia and Poinsettia cultivars (935, 1428), barley and wheat varieties (685-687, 1055), tulip cultivars and their parrot mutants (1145), tomato species and mutants (847, 1107), Aegi/ops species (1304), Oryza species (984), and several plants at difTerent phylogenetic positions (53). Peroxidase isoenzymes also served to characterize avocado cultivars, to document parentages, and to detect outcrossing (1333-1335).

Although there is at present no conclusive proof that the isozyme bands are direct gene products, it is evident that each genotype has a recognizable isozyme pattern. The interspecific hybrids generally show an additive pattern of parental peroxidases, which explains the


weak activity or the absence of certain bands which are present in one parent only (Trinh et al., 1981 ; 120 l, 1470). This apparently demonstrates the mendelian inheritance of peroxidase isozymes, as originally suggested by Hoess et al. (574) and confirmed by Snyder and Hamaker (1245).

Peroxidase can be used as a biochemical marker of sex expression. Peroxidase activity is greater in gynoecious than in monoecious cucumber plants while no differences were found in isoenzyme patterns (1095). Specifie anodic peroxidases on the other hand constitute early markers of staminal differentiation in Mercurialis annua (644-646). In both types of plants however, the differences are connected with different hormones levels, and hormonal treatments inducing changes in sex expression also modify the enzyme status.

Data concerning specifie activities and isoperoxidase multiplicities in relation to the ploidy status are relatively few (II, 338, 1043, 1158, 1251). In several varieties of beets and sugarbeets which differed in ploidy level, significant differences were shown in the activity and in the number of isoenzymes (Lobotskaya et al., 1968; Platon and Ciurea, 1969; 338). In sugarbeet, polyploidy induces a higher number of isoenzymes for peroxidase but a lower number for esterase, acid phosphatase and glutamic dehydrogenase (1251). Trinh et al. (1981) working with the Nicotiana genus clearly shows an increasing gradient in number and in intensity of the peroxidase bands from the hypohaploids to the diploids. The previously mentioned qualitative differences (1081) should be reevaluated since the absence of one band may simply be due to the low concentration of the isoenzyme in the extract. It is important to note (Trinh et al., 1981) that the ploidy-related differences are only detectable when the same chronological and physiological stages are taken into account. The most striking example of this is in the case of the hypohaploids which develop aIl the bands present in the haploids and diploids when increasing in age and remaining vegetative.

Results of peroxidase analyses in tomato plants (II) suggest that the gene expression of the double gene dosage is enhanced in sorne cases and depressed in others, resulting in a more unfavourable balance of the metabolic processes. Furthermore using tomato mutants, Soressi et al. (1248, 1249) concluded that the zymograms and total peroxidase activities were not significantly correlated with a particular plant or leaf trait. It may be inferred that mutations may influence directly or indirectly the level of peroxidase activity without affecting the genes which code for the peroxidase isozymes themselves.

PRACTICAL APPLICATIONS 125

In the Datura tetraploid, an isogenic and chromosomally 'balance type', Smith and Conklin (1981) found no change from the diploid in peroxidase activity. A genetic interpretation consistent with the resuIts would be that the enhanced activity due to an increase in dosage of the structural gene(s) is balanced by an increased production of repressor(s) of gene activity, due to an increased dosage of regulatory genes. This, together with the results of Trinh et al. (1981), shows how difficult the interpretation of isozyme profiles can be, if factors such as inheritance, ploidy leveland physiological state are not taken into account.

We have mentioned earlier the role of peroxidase in fruit development. Consequently, it has been considered as a possible parameter of ripening and senescence (471).

A number of investigators have correlated the production of viny or straw-Iike flavors to peroxidase activity. Arising from the studies of Gardner et al. (1969), modification of peroxidase activity could thus be a criterion of (loss of) quality in foods inadequately processed, including corn products.

From the previously discussed relationship between peroxidase (mainly cathodic forro), capacity of growth, and auxin availability for growth, it has been suggested that peroxidase could have a possible predictive value for sugarbeet. Peroxidase activity has been a suitable parameter for establishing the degree of superiority among seedlings of new sugarbeet hybrids, since a correlation was established between the activity of the enzyme, the mean fresh weight and the sugar yield (338, 435, 1251). A similar relationship of peroxidase activity with grain weight has been established for different varieties of bread wheat (1230).

Peroxidase has also been cited as a screening parameter for difJerent physiological stresses. An elevated peroxidase Ievel is induced by cold (Gerloff et al., 1967; Highkin, 1967; De Jong et al., 1968), drought (Stutte and Todd, 1967; Viera-de-Silva, 1968), hypoxia (Siegel et al., 1966) and salt stress (Strogonov, 1964; Rakova et al., 1969; 1273).

Peroxidase activity can also be taken as an indicator of diffèrent ion status (55, 98), deficiency (307, 1140) or toxicity (913) and as a biochemical marker for different types of pollution (263, 395, 733, 811, 839, 1329). Plant peroxidases have often been used as a marker for studying the response of plants to severaI air pollutant~. Fluoride (Lee et al., 1966; 670, 672, 759, 1048), ozone (Dass and Weaver, 1968; 262, 263, 285, 359), S02 and N02 (579, 580), lead (811), zinc (946) or gaseous HCI (359) were reported to have an effect on the


level of peroxidase activity of several plant species. Peroxidases are generally considered to be the most sensitive indicator of pollutants in the absence of visible injury. The most commonly observed response of peroxidases to poll,ution is an increase of their activity. In a few cases, sorne effect on the isoperoxidase profile was reported (262, 263, 285, 811). Peroxidases have proven useful in determining areas where plants were affected by F-containing exhausts of an aluminium smelter (670). It was possible to detect hidden injury in several tree species before the appearance of any visible symptom. Peroxidase activity also allows one to measure the effect of pollution on plants in the vicinity of a highway (395). It was also clearly established that in streets with an intense motor traille, Sedum album leaves exhibited maximum peroxidase activity when traille was maximum (l87a). In that case, the time of the higher peroxidase activity was weIl correlated with the time of higher concentration of air pollutants (CO, NO, S02)'

Increased peroxidase activity resulting from an exposure to pollutants does not appear to be a general mIe. As an example, great differences in peroxidase activity have been found in pine needles of 58 families growing at differing distances from zinc-works (946). These different reactions, which reduce the diagnostic value of peroxidase activity, could be dependent on genetic characters. In addition, Endress et al. (359) observed that peroxidase activity levels may be elevated by subjecting plants to air pollutant stress. However, the activity was also sensitive to the internaI physiological conditions of the plants. The author came to the conclusion that due to its extreme sensitivity peroxidase activity was not a reliable indicator of pollutant stress.

The reason why plant peroxidases are more active under pollution is not known. Several comparisons may be made between the reaction of peroxidases to pollution and to infection. For example, upon ozone exposure, the peroxidase activity of an ozone-tolerant cultivar of soybean is less affected than the activity of an ozone sensitive cultivar (263). This may be compared to the differences observed between resistant and susceptible plants (see Section 53). In the same way, peroxidase reaction to air pollution often exhibits cornmon features with that observed after infection (285, 482). Finally, plants already exposed to a pollutant appear to be less responsive to a new exposure as compared to plants coming from a non-polluted environment (580). This resembles the acquired resistance following an infection.

PRACTICAL APPLICATIONS 127

In animaIs too peroxidase activity can be taken as an indicator of pollution. As an example, effects of sorne industrial pollutants and factory effluents on fish kidney peroxidase activity were recorded in Ophicephalus punctatus and Clarias batrachus (911).

Extreme anodic and cathodic peroxidases have been involved both in inductive and initiative processes of root formation (see Section 5.1.2). Thus it has been proposed (449) to use their respective activities to select, from among different Asparagus plants, those individuals or segments which are most likely to succeed in rooting on a defined medium. The effectiveness of a prerooting treatment, as well as the seasonal variation in rooting ability, can be monitored using peroxidases as indicators. Thus these enzymes can be exploited as a sereening test for difJerentiating the efficiency ofchemicals in the regulation of different physiological processes.

These are a few examples of the potential practical· exploitation of peroxidase and its isozyme forms. On the basis of their participation in various physiological processes, many others can be imagined. One such possibility is the selection between disease resistant and susceptible types (see Section 5.3). However, to date the potential diagnostic application of peroxidases remains unfulfilled.

In addition to their applications in physiological and genetical studies, peroxidases are widely used as tracers in neurology and for the immunodetection of a great number of molecules. These two subjects account for a great part of the papers dealing with peroxidases but are not covered by the present book.


REFERENCES


DASS, H.C.; WEAVER, G.M. 1968. Modification of ozone damage to Phaseolus vulgaris by antioxidants, thiols and sulfbydryl reagents. CAN. J. PLANT SCI. 48: 569-574.

DE JONG, D.; OLSON, A.; HAWKER, K.; JANSEN, E. 1968. Effect of cultivation temperature on peroxidase isozymes of plant cells grown in suspension. PLANT PHYSIOL. 43: 841-844.

GARDNER, H.W.; INGLETT, G.E.; ANDERSON, RA. 1969. Inactivation of peroxidase as a function of corn processing. CEREAL CHEM. 46: 626-634.

GERLOFF, E.; STAHMANN, M.; SMITH, D. 1967. Soluble proteins in Alfalfa roots as related to cold hardiness. PLANT PHYSIOL. 42: 895-899.

HIGHKIN, H.R 1967. Effect of temperature on formation of peroxidase isozymes. PLANT PHYSIOL. SUPPL. 42: S 16.

LEE, c.J.; MILLER, G.W.; WELKIE, G.W. 1966. The effects of hydrogen fluoride and wounding on respiratory enzymes in soybean leaves. AIR WATER POLLUT. INT. J. 10: 169-181.

LOBOTSKAy A, L.; BYEKKO, Y.A.; PALCHENKO, L.A.; BORMOTOV, V.Y. 1968. Action of peroxidase and respiration intensity in sugar beet plants with different ploidy levels (in Russian). DOKL. AKAD. NAUK. B. SSR 12: 563-565.

PLATON, M.; CIUREA, G. 1969. Etude physiologique de quelques formes polyploïdes roumaines de betterave sucrière. REV. ROUM. BIOL. 14: 309-313.

RAKOVA, N.; KLYSHEV, L.; STROGONOV, B. 1969. The effect of sodium sulfate and sodium chloride on the protein composition of pea roots. FIZIOL. RAST. 16: 22-28.

SIEGEL, S.; GIUMARRO, c.; DALY, O. 1966. Micro-aerobic capabilities in land plants: observations on survival and growth of plants submerged in fresh and saline waters. NATURE 209: 1330-1334.

129 PRACTICAL APPLICATIONS

SMITH, H.H.; CONKLIN, M.E. 1981. Effects of gene dosage on peroxidase isozymes in Datura stramonium trisomics. 3rd Int. Conf. Isozymes. Markert, c.L. (Ed.). Academic Press, New York, in press.

STROGONOV, B. 1964. Physiological Basis of Salt Tolerance in Plants. ACADEMIC SCIENCE U.S.S.R. (Davey, New York).

STUTTE, c.A.; TODD, G. 1967. Effects of water stress on soluble leaf proteins in Triticum aestivum L. PHYTON 24: 67-75.

TRINH, T.H.; GASPAR, Th.; TRAN THANH VAN, K.; MARCOTTE, J.L. 1981. Genotype, ploidy and physio10gical state in relation to isoperoxidases in Nicotiana. PHYSIOL. PLANT. 53: 153-157.

TYSON, H. 1969. Peroxidase activity in Linum usitatissimum. L. ANN. BOT. 33: 45-54.

VIERA-DE-SILVA, J. 1968. Le potentiel osmotique du milieu de culture et l'activité soluble et latente de la phosphatase acide dans le Gossypium thurberi. C.R. ACAD. Sc. PARIS 67: 729-732.

CHAPTER 7

CONCLUDING REMARKS AND PROSPECTS

Peroxidases obviously are involved in many fundamental aspects of animal and plant life. The present book is an attempt to relieve their outstanding properties. They have been a little more c!arified during these last years along with the refinement of the techniques used for the study of their physico-chemical characteristics and their physiological functions. Let us hope that more and more 'peroxidasers' will help to the understanding of what was still until recently called a true morass.

The peroxidases as a group need to be further defined in terms of their genetics, physico-chemical properties, and physiological significance. As already c!aimed by Scandalios (1150) for isozymes in general, a precise definition of the basis for peroxidase multiplicity is a necessary prerequisite to the understanding of the significance of spatial and temporal isoperoxidase fluctuations encountered in plant development. It is now obvious, and everybody must be aware, that

. the appearance or disappearance of isoperoxidases during development or in the course of a physiological process does not a priori reflect gene action in the sense of transcription. It does reflect the expression of genetic information, however, and the regulation of such difTerential gene activity can be at a number of control points, as discussed in the preceding chapters.

In the immediate future, the most important questions relating to the existence of multiple 'molecular' forms of peroxidase concern their role in cellular metabolism and difTerentiation. Information as to their biochemical and physiological functions came through the knowledge

!::~;:::.::

i~~t~~~~~


of the factors determining the basis of their subcellular distribution. together with a thorough investigation of their physico-chemical properties. Although catalytic functions may be similar, kinetic differences may allow flexibility in biological role.

In many instances, peroxidases have proven useful as indicators or markers of the reactions of plants to external stimuli such as light, prickings, rubbings, infections or pollutions. Plants, as immobilized and autotroph organisms, are tightly dependent upon the environmental conditiOns. They must often adjust themselves very quickly to external changes through elastic or plastic modulations of their functioning. This reactivity cannot be achieved through sole long-term responses involving protein synthesis, but requires immediate and quick regulation. The former is linked to metabolite and hormone circulation, whilê the latter is linked to ion and electrochemical transport. Colloidal and microtrabecular systems, as well as membranes, play an important role in these short-term regulations, which often involve peroxidases. Intercellular or interorganismic communications, which are required in these processes, were in sorne cases visualized by rapid qualitative or quantitative changes in peroxidase activity (142, 143, 1021). ~This

reactivity of peroxidases is an additional reason for a better understanding of their regulation.

·1

OM.~ ~HVd

REFERENCES 139 0001. ABELES, EB.

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1971. enzyme

0003. ABRAMOWITZ, J.; CHAVIN, W. 1978. ln vitro effect of hormonal stimuli upon tyrosinase and peroxidase activities in murine melanomas. BIOCHEM. BIOPHYS. RES. COMM. 85: 1067-1073.

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0007a. AHMED, S. 1980. Effect of different oxygen pressures and of age on changes in catalase and peroxidase activities of Rhizopus oryzae under high pressures of oxygen. PAKISTAN J. BOT. 12: 69-76.

0008. AHUJA, B.S.; SARMA, TA; KIRAN, U.; SUDERSHAN. 1980. Activities of superoxide dismutase and peroxidase enzymes during early phase of germination in mung bean (Phaseolus aureus). INDIAN J. BIOCHEM. BIOPHYS. 17: 77-79.

0009. AHUJA, M.R.; GUPTA, V.K. 1974. Control oftumour-associated peroxidases in a genetic tumour system in Nicotiana. EXPERIENTIA 30: 1007-1008.

0010. AL-AZZAWI, M.J.; HALL, J.L. 1977. Effects of adenosine triphosphatase and peroxidase activities ANN. BOT. 41: 431-435.

aldehyde in maize

fixation on root tips.

:.

0011. ALBUZIO, A.; SPETTOLI, P.; CACCO, G. 1978. Changes in gene expression from diploid to autotetraploid status of Lycopersicon esculentum. PHYSIOL. PLANT. 44: 77-80.

0012. ALEXANDER, N.M. 1974. Oxidative c1eavage of tryptophanyl peptide bonds during chemical and peroxidase-catalyzed iodinations. ENG. J. BIOL. CHEM. 249: 1946-1952.


0013. ALEXANDRESCU, V.; HAGIMA, 1.; POPOV, D.; JULAVEANU, A. 1975. Multiple molecular forms of catalase, peroxidase and acid phosphatase in Lycopersicum sp. with genetical and induced resistance againt tobacco mosaic virus (TMY). REV. ROUM. BIOCHIM. 12: 209-212.

0014. ALEXANDRESCU, V.; HAGIMA, 1.; SAULESCU, N.N. 1979. Peroxidase genetic variants in seeds ofsorne Triticum aestivum cultivars. REV. ROUM. BIOCHIM. 16: 167-174.

0015. ALEXANDRESCU, V.; NICOLAE, S. 1979. Genetic variants of peroxidase . in sorne species related to common wheat (Triticum aestivum, L.).

REV. ROUM. BIOCHIM. 16: 247-254.

0016. ALFSEN, A.; CHIANCONE, E.; ANTONINI, E.; WAKS, M.; WYMAN, J. 1970. Studies on the reaction of haptoglobin with hemoglobin chains. III. Observations on the kinetics of the reaction of the haptoglobin hemoglobin complexes with carbon monoxide. BIOCHIM. BIOPHYS. ACTA 207: 395.

0017. ALGHISI, P.; LENNA, D.; MAGRO, P. 1971. Ricerche sull'ossidasi dell'acido indolacetico in piante sane e ammalate. Il. Purificazione e confronto delle attirita AIA ossidasica e perossidasica in piante sane di mais suscettibili e resistenti all'Ustilago zeae. RIV. PATHOL. VEG. 3: 189-202.

0018. ALI, A.; FLETCHER, R.A. dominance in soybeans.

1971. Hormonal interaction in controlling apical CAN. J. BOT. 49: 1727-1731.

0019. ALI, M.R.; CARUSO, J.L. 1976. Morphogenetic aspects of a leatless mutant in tomato. J. EXPT. BOT. 27: 942-946.

0020. AUBERT, G.; RANJEVA, R.; BOUDET, A.M. 1977. Organisation subcellulaire des voies de synthèse des composés phénoliques. PHYSIOL. VEG. 15: 275-301.

0021. ALMGARD, G. 1974. Electrophoresis as an aid testing. SEED. SCI. TECHNOL. 2: 260-261.

to identification in seed

0022. ALMGARD, G.; CLAPHAM, D. 1975. Isozyme variation distinguishing 18 Avena cultivars grown in Sweden. SWEDISH J. AGRIe. RES. 5: 61-67.

0023. ALMGARD, G.; CLAPHAM, D. 1977. Swedish wheat cultivars distinguished by content ofgliadins and isozymes. SWEDISH J. AGRle. RES. 7: 137-142.

0024. ALMGARD, G.; LANDEGREN, U. the identification ofbarley cultivars.

1974. Isoenzymatic variation used for Z. PFLANZENZÜCHTG. 72: 63-73.

0025. ALMGARD, G.; NORMAN, T. 1970. Biochemical. technique as an aid to distinguish sorne cultivars of barley and oats. AGRle. HORT. GENET. 28: 117-123.

0026. ANDERSON, L.e.; SHAPIRO, B.L. 1979. The elfect of alloxan diabetes and insulin in vivo on peroxidase activity in the rat submandibular gland. ARCH. ORAL BIOL. 24: 343-346.

141REFERENCES

0027. ANDERSON, W.A.; BURNETT, C. 1979. Reproductive tract peroxidase as end products of estrogen-specific gene expression. J. HISTOCHEM. CYTOCHEM. 27: 1363-1364.

0028. ANDERSON, W.A.; TRANTALIS, J.; KANG, Y.H. 1975. Ultrastructural localization of endogenous mammary gland peroxidase during lactogenesis in the rat. Results after tannic acid-fonnaldehyde-glutaraldehyde fixation. J. HISTOCHEM. CYTOCHEM. 23: 295-302.

0029. ANDREEVA, VA; VORONOVA, VA; UGAROVA, N.N. 1979. Activity, . isoenzyme spectrum, thennal stability and molecular weight of peroxidase

isolated from healthy and virus-infected tobacco plants. BIOKHIM. 44: 309-313.

0030. ANST1NE, W.; JACOBSEN, J. V.; SCANDALIOS, J.G.; VARNER, J.E. 1970. D, 0 as a density label of peroxidase in genninating barley embryos. ptANT PHYSIOL. 45: 148-152.

0031. ANTAKLY, T.W.; TANAKA, S.; OH KAWA, K.I.; BERNHARD, W. 1979. Cytochemica1 localization of peroxidase and peroxidase- 1abelled antibodies in ultrathin frozen sections. CELL. MOL. BIOL. 24: 205-212.

0031a. ARA1S0, T.; DUNFORD, H.B. 1980. Horseradish peroxidase. XLI. Complex fonnation with nitrate and its effect upon compound 1 fonnation. BIOCHEM. BIOPHYS. RES. COMM. 94: 1177-1182.

0032. ARAISO, T.; DUNFORD, H.B.; CHANG, C.K. 1979. Horseradish peroxidase. XXXVII. Compound fonnation from reconstituted enzyme lacking free carboxyl groups as heme side chains. BIOCHEM. BIOPHYS. RES. COMM. 90: 520-524.

0033. ARAISO, T.; YAMAZAKI, 1. 1978. Kinetic analysis of the acid-alkaline conversion of horseradish peroxidases. BIOCHEM. 17: 942-946.

0034. ARAKAWA, H.; MAEDA, M.; TSUJI, A. 1979. Chemiluminescence enzyme immunoassay of cortisol usinE peroxidase as label. ANAL. BIOCHEM. 97: 248-254.

0035. ARMSTRONG, D.; RINEHART, R.; DIXON, L.; REIGH, D.L. 1978. Changes of peroxidase with age in Drosophila. AGE 1: 8-12.

0036. ARNISON, P.G.; BOLL, W.G. 1974. Isoenzymes in cell cultures of bush . bean (Phaseolus vulgaris cv..Contender): isoenzymatic changes during the callus cycle and differences between stock cultures. CAN. J. BOT. 52: 2621-2629.

0037. ARNISON, P.G.; BOLL, W.G. 1975. Isoenzymes in cell cultures of bush bean (Phaseolus vulgaris cv. Contender): isoenzymatic differences between stock suspension cultures derived from a single seedling. CAN. J. BOT. 53: 261-271.


0038. ARNISON, P.G.; BOLL, W.G. 1976. The effect of 2,4-D and kinetin on the morphology, growth and cytochemistry of peroxidase of cotyledon cell suspension cultures of bush bean (Phas('olus vulKaris cv. Contender). CAN. J. BOT. 54: 1847-1856.

0039. ARNISON, P.G.; BOLL, W.G. 1976. The effect of 2,4-D and kinetin on peroxidase acivity and isoenzyme pattern in cotyledon suspension cultures of bush bean (Phaseolus vulgaris cv. Contender). CAN. J. BOT. 54: 1857-1867.

0040. ARNISON, P.G.; BOLL, W.G. 1978. The effect of 2,4-D and kinetin on the activity and isoenzyme· pattern of various enzyme in cotyledon cell suspension cultures of bush bean (Phaseolus vulgaris cv. Contender). CAN. J. BOT. 56: 2185-2195.

0041. ASADA, K.; TAKAHASHI, M. J971. Purification and properties ofcytochrome c and two peroxidases from spinach Ieaves. PLANT CELL PHYS/OL. 12: 361-375.

0042. ATSUMI, S. ; HAYASHI, T. 1978. The relationship between auxin concentration, auxin protection and auxin destruction in crown gall cells cultured in vitro. PLANT CELL PHYSIOL. 19: 1391-1397.

0043. AULIKKl, M.S.; MIKlLA, J.J. J975. Activities of two peroxidases in resting and germinating seeds of scots pine, Pinus sylves/ris. PHYSIOL. PLANT. 33: 261-265.

0044. AUNE, T.M.; THOMAS, E.L. 1978. Oxidation of protein sulfhydryls by products of peroxidase-catalyzed oxidation of thiocyanate ion. BIOCHEM. 17: 1005-1009.

0045. AVER'YANOV, A.A.; MERZLYAR, M.N.; RUBIN, B.A. 1978. Chemiluminescence in the oxidation of gossypoJ by peroxidase. BIOKHIM. 43: 1255-1259.

0046. AVRAMEAS, S.; GUIBERT, B. 1972. Enzyme-immunoassay for measurement of antigens using peroxidase conjugates. BIOCHIMIE 837-842.

the 54:

0047. AWASTHI, Y.G.; BEUTLER, E.; SRIVASTAVA, K. 1975. Purification and properties of human erythrocyte gJutathione peroxidase. J. BIOL. CHEM. 250: 5144-5149.

0048. AZEN, E.A. 1978. Salivary peroxidase activity and thiocyanate concentration in human subjects with genetic variants of salivary peroxidase. ARCH. ORAL BIOL. 23: 801-806.

0049. BADEN, D.G.; CORBETT, M.D. 1979. Peroxidases produced by the marine sponge fa/rocha/a birotulata. COMP. BIOCHEM. PHYSIOL. 64: 279-284.

0050. BADEN, D.G.; CORBETT, M.D. 1980. Bromoperoxidase from Penicillus capitatus, Penicillus lamourouxii and Rhipocephalus phoenix. BIOCHEM. J. 187: 205-211.

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0051. BAJAJ, Y.P.S.; BAJAJ, S.; BOPP, M. difTerentiation in plant tissue cultures.

1972. Peroxidases in relation AMER. J. BOT. 59: 668-672.

to

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0188. CATALFAMO, J.L.; FEINBERG, J.H.; SMITH, G.W.; BIRECKA, H. 1978. Effect of gibberellic acid and ethylene on peroxidase in pea intemodes. J. EXP. BOT. 29: 347-358.

0189. CATEDRAL, F.; DALY, J.M. 1976. Partial characterization of peroxidase isoenzymes from rust-affected wheat Jeaves. PHYTOCHEM. 15: 627-631.

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0194. CHAN, K.Y.; BUNT, A.H.; HASCHKE, R.H. 1980. Endocytosis and compartmentation of peroxidases and eationized ferritin in neuroblastoma. J. NEUROCYTOL. 9: 381-404.

0195. CHANCE, B. reactions.

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0215. CHIBBAR, R. N.; GURUMURTI, K.; NANDA, K K 1980. Effect of maleic hydrazide on peroxidase isoenzymes in relation to rooting hypocotyl cuttings of Phaseolus mungo. BIOL. PLANT. 22: 1-6.

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0217. CHILDS, RE.; BARDSLEY, W.G. 1975. The steady-state kinetics ofperoxidase with 2,2'-azinobis (3-ethyl-benzothiazoline-6-sulphonic acid) as chromogen. BIOCHEM. J. 145: 93-103.

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0222. CHOUREY, P.S.; SMITH, H.H.; COMBATTI, N.e. 1973. Effects of X irradiation and indoleacetic acid on specific peroxidase isoenzymes in pith tissue of a Nicotiana amphiploid. AMER. J. BOT. 60: 853-857.

0223. CHOY, Y.M.; WONG, Y.S.; LAU, KM.; YUNG, KH. 1979. Thermal activation of peroxidase from tobacco leaf mesophyll cell walls. INT. J. PEPTIDE PROTEIN RES. 14: 1-4.

0224. CHRISTIE, K N.; STOWARD, P.J. 1978. Endogenous peroxidase in mast cells localized with a semipermeable membrane technique. HISTOCHEM. J. 10: 425-434.

0225. CHRISTIE, K.N.; STOWARD. P.J. 1979. Specificity of cytochemical procedures for localizing peroxidase activity in the sarcoplasmic reticulum. HISTOCHEM. 64: 315-318.

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0280. DARIMONT, E.; GASPAR, T. 1972. A propos du nombre et du poids moléculaire des isoenzymes peroxydasiques de la racine de Lens culinaris. SOc. BOT. FR. MEMOIRES (Coll. Morpho!.), pp. 211-222.

0281. DARIMONT, E.; GASPAR, l'.; HOFINGER, M. 1971. Auxin-kinetin interaction on the lentil root growth in relation to indoleacrylic acid metabolism. Z. PFLANZENPHYSIOL. 64: 232-240.

0282. DARIMONT, E.; PENEL, c.; AUDERSET, G.; GREPPIN, H.; GASPAR, T. 1977. Peroxydases de haut poids moléculaire identifiées à des peroxydases membranaires chez la Lentille. ARCH. INTERNAT. PHYSIOL. BIOCHIM. 85: 497-507.

0283. DARIMONT, E.; SCHWACHHOFER, K.; GASPAR, T. 1973. Isoperoxydases et hydroxyproline dans les parois cellulaires des racines de Lentille. BIOCHIM. BIOPHYS. ACTA 321: 461466.

0284. DASHEK, W.V.; ERICKSON, S.S.; HAYWARD, D.M.; LlNDBECK, G.; MILLS, R.R. 1979. Peroxidase in cytoplasm and cell wall of germinating lily pollen. BOT. GAZ. 140: 261-265.

0285. DASS, H.C.; WEAVER, G.M. 1972. Enzymatic changes in intact leaves of Phaseolus vulgaris following ozone-fumigation. ATM. ENVIRONM. 6: 759-763.

0286. DAUSSANT, J. 197 J. Immunochemical characterization of protein in plant studies. AGRIC. AND FOOD CHEM. 19: 653-659.


0287. DAUSSANT, J.; ROUSSAUX, J.; MANIGAULT, P. 1971. Caractérisations immunochimiques de deux auxines oxydases extmites de tumeurs végétales. FEBS LETTERS 14: 245-250.

0288. DAVIDSON, B.; SOOBACK, M.; STROUT, H.V.; NEARY, J.T.; NAKAMURA, C; MALOOF, F.F. 1979. Thiourea and cyanamide as inhibitors of thyroid peroxidase. Role of iodide. ENDOCRINOL. 104: 919-924.

0289. DAVIES, D.M.; JONES, R.; MANT LE, D. 1976. The kinetics of formation of horseradish peroxidase compound 1 by reaction with peroxobenzoic acids, pH and peroxoacid substituent effects. BIOCHEM. J. 157: 247-253.

0291. DEGN, H. 1973. Chemiluminescence in oscillatory oxidation reactions catalyzed by horseradish peroxidase. In 'BIOLOGICAL AND BIOCHEMICAL OSCILLATORS'. Lance, 8.; Pye E.K.; Ghosh, A.K.; Hers, 8. (Eds). Academic Press, New York, pp. 97-108.

0292. DE GREEF, JA; VAN HOOF, R.; CAUBERGS, R. 1977. Light-induced changes in auxin metabolism during hook opening of etiolated bean seedlings. BIOCHEM. SOC TRANS. 5: 1049-1051.

0293. DEIMANN, W.; FAHIMI, H.D. 1978. Peroxidase cytochemistry and ultrastructure of resident macrophages in fetal rat liver. A developmental study. DEVELOPM. BIOL. 66: 43-56.

0294. DE JONG, D. W. 1972. Detergent extraction of enzymes from tobacco leaves varying in maturity. PLANT PHYSIOL. 50: 733-737.

0295. DE JONG, D. W. 1973. Effect of temperature and daylength on peroxidase and malate (NAD) dehydrogenase isoenzyme composition in tobacco leaf extracts. AMER. J. BOT. 60: 846-852.

0296. DEKOCK, P.C; HALL, A.; INKSON, R.H.E. 1979. A study of peroxidase and catalase distribution in the potato tuber. ANN. BOT. 43: 295-298.

0297. DEKOCK, P.C; VAUGHAN, D. 1975. Effects of sorne chelating and phenolic substances on the growth of excised pea root segments. PLANTA 126: 187-195. .

0298. DELINCEE, H.; RADOLA, 8.J. 1970. Thin-layer isoelectric focusing on Sephadex layers of horseradish peroxidase. BIOCHIM. BIOPHYS. ACTA 200: 404-407.

0299. DELINCEE, H.; RADOLA, 8.J. 1971. Isoelectric fractionation of horseradish peroxidase. In 'PROTIDES OF BIOLOGICAL FLUIDS'. Proc. 18th Colloq., Brugge. Pergamon Press, Oxford, pp. 493-497.

0300. DELINCEE, H.; RADOLA, B.J. 1972. Detection of peroxidase by the print technique in thin-layer isoelectric focusing. ANAL. BIOCHEM. 48: 536-545.

0301. DELINCEE, H.; RADOLA, B.J. 1975. Fractionation of HRP by preparative isoelectric focusing, gel chromatography and ion-exchange chromatography. EUR. J. BIOCHEM. 52: 321-330.

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0303. DELINCEE, H.; RADOLA, 8.1.; DRAWERT, F. on the isoelectric and size properties of EXPERIENTIA 27: 1265-1267.

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0304. DELINCEE, H.; RADOLA, B.J.; DRAWERT, F. 1973. The effect ofcûmbined heat and irradiation treatment on the isoelectric and size properties of horseradish peroxidase. ACTA ALIMENTARIA 2: 259-274.

0305. DELINCEE, H.; SCHAFER, W. 1975. Der Einfluss thermischer Behandlung von Spinat in Temperaturbereich bis 100' auf den Gehalt an wesentlichen Inhaltsstoffen. VII. Mitteilung: Hitzaktivierung von Peroxydase Isozymen in Spinat. LEBENSM. WISS. TECHNOL. 8: 217-221.

0306. DELRIO, LA; GOMEZ, M.; LOPEZ-GORGE, 1. 1977. Catalase and peroxidase activities, chlorophyll and proteins during storage of pea plants at chilling temperatures. REV. ESP. FISIOL. 33: 143-148.

0307. DELRIO, LA, GOMEZ, M., YANEZ, J.; LEAL, A.; LOPEZ-GORGE, 1. 1978. Iron deficiency in pea plants. Effect on catalase, peroxidase, chlorophyll and proteins of leaves. PLANT SOIL 49: 343-353.

0308. DEMIREVSKA-KEPOVA, K.;' BAKARDJIEVA, N.T. 1976. Study on competition between guaiacol and ascorbic acid in peroxidase reaction and on ion effects by means of absorption spectra. CAN. J. BOT. 54: 90-99.

0309. DEMOREST, D.M.; STAHMANN, MA 1972. The binding of the peroxidase oxidation products ofindole-3-acetic acid to histone. BIOCHEM. BIOPHYS. RES. COMM. 47: 227-233.

0310. DENCHEVA, AV.; DOUSHKOVA, P.I.; KLISURSKA, D.Y. 1974. Influence of gibberellic acid and of the maleic hydrazide on the peroxidase in Senedesmus obliquus (Turp) Kütz. C.R. ACAD. BULG. Sc. 27: 703-706.

0311. DENCHEVA, AV.; KLISOURSKA, D.Y. 1976. Activity and isoenzyme composition of the peroxidase in the zones of growth and differentiation of the cells in shoots of maize. C.R. ACAD. BULG. SCI. 29: 1179-1182.

0312. DENDSAY, J.P.S.; SACHAR, R.C. 1978. Honnonal control of peroxidase activity in germinating mung bean cotyledons. PHYTOCHEM. 17: 1017-1019.

0313. DENNA, D.W.; ALEXANDER, M.8. 1975. The isoperoxidases ofCucurbita pepo L. In 'ISOZYMES. II. PHYSIOLOGICAL FUNCTION'. Markert, c.L. (Ed.). Academie Press, New York, pp. 851-864.

0314. DE OLMOS, J.S. 1977. nervous connections.

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0315. DE RYCKER, J.; HALLIWELL, B. 1978. Oxidation of 2-nitropropane by horse radish peroxidase. Involvement of hydrogen peroxide and ofsuperoxide in the reaction mechanism. BIOCHEM. J. 175: 601-606.

0316. DESOMBRE, E.R.; ANDERSON, W.A.; KANG, Y.-H. 1975. Identification, subcellular localization, and estrogen regulation of peroxidase in 7,12dimethylbenzo(a)anthracene - induced rat mammary tumors. CANCER RES. 35: 172-179.

0317. DE SOMBRE, E.R.; LYTTLE, e.R. 1978. Isolation and purification of rat mammary tumor peroxidase. CANCER RES. 38: 4086-4090.

0318. DESSER, R.K.; HIMMELHOCH, S.R.; EVANS, W.H.; JANUSKA, M.; MAGE, M.; SHELTON, E. 1972. Guinea pig heterophil and eosinophil peroxidase. ARCH. BIOCHEM. BIOPHYS. 148: 452-465.

0319. DEVI, G.; SHAILA, M.S.; RAMAKRISHNA, T.; GOPINATHAN, K.P. 1975. The purification and properties of peroxidase in Myobacterium tuberculosis H37Rv and its possible role in the mechanism of action of isonicotine acid hydrazide. BIOCHEM. J. 149: 187-197.

0320. DEWOLF, M.; HILDERSON, H.J.; LAGROU, A.; DIETRICK, W. 1977. Peroxidase, a marker enzyme for rough endoplasmic reticulum in bovine thyroid. ARCH. INTERNAT. PHYSIOL. BlOCHIM. 85: 971-974.

0321. DEZSI, L. 1975. Changes of glycolic acid oxidase and peroxidase activity in maize leaves during the vegetation period. ACTA AGRON. ACAD. SC\. HUNG. 24: 305-314.

0322. DEZSI, L.; PALFI, G.; FARKAS, G.L. 1970. increase in peroxidase activity in diseased PHYTOPATHOL. Z. 69: 285-291.

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0323. DHALIWAL, G.; BHATTACHARYA, N.e.; NANDA, K.K. 1974. Promotion of rooting by cycloheximide on hypocotyl cuttings in Impatiens balsamina and associated changes in the pattern of isoperoxidases. INDIAN J. PL. PHYSIOL. 17: 73-81.

0324. DHAWAN, A.K.; MALIK, e.P. 1979. Cyclic-AMP control of sorne oxidoreductases during pine pollen gennination and tube growth. PHYTOCHEM. 18: 2015-2017.

0325. DICKS, J.W. 1970. The participation of peroxidase and oxalic acid in crocin destruction by a particulate system from sugar beet leaves. PHYTOCHEM. 9: 1433-1441.

0326. DIMITRIJEVIC, L.; AUSSEL, c.; MUCCHlELLl. A.; MASSEYEFF, R. 1979. Purification and characterization of an estrogen binding peroxidase from human fetuses. BIOCHIMIE 61: 535-542.

0327. DINELLO, R.K.; DOLPHIN, D. 1978. Interaction of the hemin :2 and 4 substituents with apo horseradish peroxidase. BIOCHEM. BIOPHYS. RES. COMM. 80: 698-703.

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0329. DOLMAN, D.; NEWELL, P.A.; THURLOW, M.D.; DUNFORD, H.B. 1975. A kinetic study of the reaction of horseradish peroxidase with hydrogen peroxide. CAN. J. BIOCHEM. 53: 495-501.

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0331. DOUMENJOU, N.; MARIGO, G. 1978. Relations polyphenols-croissance: rôle de l'acide chorogénique dans le catabolisme auxinique chez Lycopersicum esculentum. PHYSIOL. VEG. 16: 319-361.

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in

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0342. DUMITRESCU, M.; GORENFLOT, R.; COUDERC, H. 1975. La présence d'un inhibiteur de la peroxidase dans la gousse sèche de l'Anlhy/lis vulnl'ria L. ssp. di/lenii. REV. ROUM. BIOCHIM. 12: 15-20.

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0349. DURAN, N.; FALlONl, A. 1978. Singlet oxygen formation during peroxidase catalyzed degradation of carcinogenic N-nitrosamine. BIOCHEM. BIOPHYS. RES. COMM. 83: 287-294.

0350. DURAN, N.; ZINNER, K.; VIGIDAL, c.c.c.; CILENTO, G. 1977. Generation of eiectronically excited aromatic aldehyde in the peroxidase catalyzed aerobic oxidation of aromatic acetaldehydes. BIOCHEM. BIOPHYS. RES. COMM. 74: 1146-1153.

0351. DUVAL, J.c.c. 1974. Etude polarographique de l'activité mitochondriale en présence de diaminobenzidine. C.R. ACAD. Sc. PARIS 278: 257-260.

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0369. ESTERBAUER, H.; GRILL, D.; ZOTTER, M. 1978. Peroxidase in needles of Picea abies L. Karst. BIüCHEM. PHYSIOL. PFLANZ. 172: 155-160.

0370. EVANS, J.J. 1970. Spectral similarities and kinetic differences of two tomato plant peroxidase isoenzymes. PLANT PHYSIOL. 45: 66-69.

0371. EVANS, J.J.; MECHAM, D.K. 1971. Occurence and properties ofperoxidase isoenzymes in wheat flour and milling fractions. (Abstr). CEREAL SCI. TODAY 16: 22.

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0373. EVANS, M.L.; RAY, P.M. 1973. Inactivity of 3-methyleneoxindole as mediator ofauxin action of ceIJ elongation. PLANT PHYSIOL. 52: 186-189.

0374. FACCIOLI, G. 1979. Relation of peroxidase, catalase and polyphenoloxidase to acquired resistance in plants of Chenopodium amaranticolor locally infected by tobacco necrosis virus. PHYTOPATHOL. Z. 95: 137-149.

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0376. FAHIMI, H.D. 1979. An assessment of the DAB methods for cytochemical detection of catalase and peroxidase. J. HISTOCHEM. CYTOCHEM. 27: 1365-1366.

0377. FAHIMI, H.D.; HERZOG, V. 1973. A colorimetrie method for measlirement of the (peroxidase-mediated) oxidation of 3,3'-diaminobenzidine. J. HISTOCHEM. CYTOCHEM. 21: 499-502.

0378. FAVILLA, R.; CAVATORTA, P. 1975. Peroxidase activity of horse liver alcohol dehydrogenase in the presence of J3-NAa- and hydrogen peroxide. FEBS LETTERS 50: 324-329.

0378a. FEDAK, G.; RAJHATHY, T. 1972. CAN. J. PLANT SCI. 52: 751-756.

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0427. GAS, c.; RETHORE, J.L.; FALLOT, J. 1974. Mise en évidence et caractérisation de plusieurs composés de type 'protecteurs d'auxine' dans les extraits de parenchyme vasculaire de tubercules de Topinambour. C.R. ACAD. Sc. PARIS 278: 1561-1564.

0428. GASPAR, T. 1970. Effet comparé de l'Amo-1618 et de l'AIA sur les peroxydases ribosomiques et cytoplasmiques de la racine de Lentille. PHYSIOL. VEG. 8: 641-648.

0429. GASPAR, T. 1970. Dégradation de l'acide p-indolylacrylique par le système peroxydase-acide p-indolylacétique en l'absence de peroxyde exogène. C.R. ACAD. Sc. PARIS 271: 928-932.

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0454. GEIGER, J.P.; GOUJON, M. 1977. Etude de deux peroxydases différentes extraites des tissus racinaires d'Hévéas sains et parasités par Leptorus lignosus (KI.) Heim. e.R. ACAD. Se. PARIS 284: 1053-1056.

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,

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'~

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'."

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'.:'

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l"

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----

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~: : .

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f'

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0773. LOCKHART, B.E.; SEMANCIK, J.S. 1970. Orowth inhibition, peroxidase and 3-indoleacetic acid oxidase activity, and ethylene production in cowpea mosaic virus-infected cowpea seedlings. PHYTOPATHOL. 60: 553-554.

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0798. MACPHIE, J.L. 1979. Peroxidase activity in non-parenchymal cells isolated from rat liver : a cytochemical study. ACTA HEPATO-GASTROENROL. 26: 442-445.

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J

0802. MADER, M. j 980. Origin of the heterogeneity of peroxidase isoenzymes group GL from Nicotiana labacum. 1. Conformation. Z. PFLANZENPHYSIOL. 96: 283-296.

0803. MADER, M.; BOPP, M. 1976. Neue Vorstellungen zum Problem der Isoperoxidasen anhand der Trennung durch Disk-Elektrophoresis und Isoelektrische Fokussierung. PLANTA 128: 247-253.

/',/

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0817. MALTEMPO, M.M.; OHLSSON, P.-I.; PAUL, K.G.; PETERSSON, L.; . EHRENBERG, A. 1979. Electron paramagnetic resonance analyses of horseradish peroxidase in situ and alter purification. BIOCHEM. 18: 2935-2941.

0818. MANES, M.E. 1973. Actividad de polyfenol oxidasa e indol acetico oxidasa de peroxidasas separadas por electroforesis. PHYTON (BUENOS AIRES) 31: 79-84.

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0822. MARAITE, H. 1973. Changes in polyphenoloxidases and peroxidase in muskmelon (Cucumis mela L.) infected by Fusarium axysporum f. sp. melanis. PHYSIOL. PLANT PATHOL. 3: 29-49.

0823. MARANI, E.; RIETVELD, W.J.; OSSELTON, J.c. 1979. Ultrastructural localization of the endogenous peroxidase activity in the ventromedial arcuate nucleus. IRCS MED. SCI. BIOCHEM. 7: 501-504.

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0825. MARIE, J.P.; VERNANT, J.P.; DREYFUS, 8.; BRETON-GORIUS, J. 1979. Ultrastructural localization of peroxidases in 'unditTerentiated' blasts during the blast crisis of chronic granulocytic leukemia. BRIT. J. HAEMATOL. 43: 549-558.

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of

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1137. SACHER, J.A.; TOWER, G.J.N.; DAVIES, D.D. 1972. Effect of light and ageing on enzymes, particularly phenylalanine ammonialyase, in discs of storage tissue. PHYTOCHEM. Il: 2383-2391.

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1401. VENERE, blight.

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,-'-


1444. WITTENBACH, VA; BU KOVAC, M.J. 1975. Cherry fruit abscission : Peroxidase activity in the abscission zone in relation to separation. J. AMER. SOe. HORT. SCI. 100: 387-391.

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1477. YOUNG, O.; BEEVERS, H. castor bean endosperm.

1976. Mixed function oxidases from germinating PHYTOCHEM. 15: 379-385.

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1482. ZALEWSKA, J.; SANIEWSKI, M. 1970. Influence of morphactin IT 3456 on geotropism and activity of enzymes connected with IAA oxidation in pea seedlings. Z. NAUK. UNIV. MIKOLAJA KOPERNIKA W TORUN BIOLOGIA 13: 267.

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1484. ZIMMERMANN, H.J.; ROSENSTOCK, G. 1976. Proteingehalt, Proteinmuster, Peroxydase- und Malatdehydrogenase. Isoenzymmuster wahrend der Entwicklung und Lagerung der Knol1en von Solanum luberosum L. BIOCHEM. PHYSIOL. 169: 321-336.

1485. ZIMMERMANN, H.J.; ROSENSTOCK, G. 1976. Proteingehalt, Proteinmuster, Peroxydase- und Malatdehydrogenase. Isoenzymmuster beim Speicherparenchym von Solanum tuberosum L. nach Verwendung. BIOCHEM. PHYSIOL. PFLANZEN 169: 487-499.

1486. ZINNER, K.; DURAN, N.; VIDIGAL, c.c.c.; SHIMIZU, Y.; CILENTO, G. 1976. Chemienergized aromatic aldehyde from the peroxidase catalyzed oxidation of pyruvates: excited vanillin from vanylpyruvate. ARCH. BIOCHEM. BIOPHYS. 173: 58-65.

1487. ZMRHAL, Z.; MACHACKOVA, L 1978. Isolation and characterjzation of wheat peroxidase isoenzymes BI. PHYTOCHEM. 17: 1517-1520.

1488. ZOPPI, F.; FENILI, D. 1980. Drug interferences in reactions for detecting hydrogen peroxide by means of peroxidase. CLIN. CHEM. 26: 1229-1230.

1

. 1

1

1

AUTHORINDEX

ABE, T. : 1457. ABELES, F.B. : 1,2. ABON, C. : 258. ABRAHAMS, S.J. : 1367. ABRAMOWITZ, J. : 3.

~ :ACKERMAN, GA : 4. ADAMS, Jr. W.R. : 5. ADAMS, PA : 6. AHERN, T.J. : 7. AHFORS, C.E. : 163. AHLUWALIA, S. : 519, 519a. AHMED, S. : 7a. AHUJA, B.S. : 8. AHUJA, M.R. : 9. AKlYAMA, M : 1205. AKSENOVA, V.A : 1126. AKULOVA, E.A. : 919. AL-AZZAWI, M.J. : 10,513. ALBALA, A. : 957. ALBUZIO, A. : Il. ALCAREZ, C. : 186. ALESHIN, E.P. : 887. ALEXANDER, M.B. : 313. ALEXANDER, N.M. : 12, 702. ALEXANDRESCU, V. : 13, 14, 15,506. ALEXEEVA, V.J. : 1298. ALFSEN, A. : 16. ALGHISI, P. : 17. ALI, A. : 18. ALI, M.H. : 19. ALIBERT, E. : 20. ALLAN, G.G. : 7. ALLARD, R.W. : 234, 523, 832, 833. ALLDRIDGE, NA : 468. ALMGARD, G. : 21, 22, 23, 24, 25. AMIN, J.V. : 1232. ANDERSON, J.O. : 1371. ANDERSON, L.C : 26. ANDERSON, ·W.A. : 27, 28, 175, 227, 316.


ANDREEVA, VA : 29. ANSTINE. W. : 30. ANTAKLY, T.W. : 31,970. ANTONINI, E. : 16, \032. 1033. 1034. ANTOSZEWSKI, R. : 267. 268,440, 1134 AR, N.P. : 636. ARAISO, T. : 31a, 32, 33. 345, 1460. ARAKAWA, H. : 34. ARCENEAUX, D. : 273. ARCHER, J.M. : 1117. ARMSTRONG, A : 937. ARMSTRONG, D. : 35, 1291. ARNISSON, P.G. : 36, 37, 38, 39, 40. ARUTYUNYAN, AM. : 810. ARYA, H.C. : 1060, 1060a, 1060b, lO73a, lO73b. ASADA, K. : 41. ASADA, Y. : 967. ASAKUA, T. : 1311. ASTHANA, J.S. : 1254. ATACK, AV. : 1154, 1155. ATAULLAKHANOV, F.l. : 379. ATSUMI, S. : 42. AUDERSET, G. : 282, 479. AUGUSTO, O. : 228. AULIKKI, M.S. : 43. AUSSEL, C. : 326. AUSTIN, J.H. : 1291. AUNE, T.M. : 44, 1323, 1324. AVER'YANOV, AA : 45. AVISSE, C. : 1397. AVRAMEAS, S. ; 46, 160, 1057, 1337. AWASTHI, Y.G. : 47. AZEN, EA : 48.

BABBLE, G.R. : 1213. BABOSZEBENYI, E. : 1369. BACON, D.R. : 666. BADEN, D.G. : 49, 50. BAG, A. : 912 BAILLAUD, L. : 140. BAINTON, D.F. : 145. BAJAJ, S. : 51, 52. BAJAJ, Y.P.S. ; 51, 52. BAKARDJIEVA, N.T. ; 52a, 54, 54a, 54b, 54c, 55, 56, 57, 58, 58a, 59, 308,460,461. BAKER, B. : 524.

257 AUTHORINDEX

BAKER, B.L. : 524 BALA, S. : 1299. BALABAEV, N.K. : 379. BALASIMHA, D. : 60, 61, 62, 63, 64, 65, 66, 1070, 1071, 1072. BALAZS, E. : 419. BALDWIN, DA : 6. BALLAL, S. K. : 1191. BANDURSKI, R.S. : 237. BANERJEE, R.K. : 204. BANERJI, A. : 67 BANERJI, D. : 1143 BANGERTH, F. : Ina. BANKSTON, P.W. : 1042 BAR-AKIVA, A. : 1140. BARBARA, D.J. : 68, 1451. BARBAS, H. : 867. BARBOTIN, J.N. : 69. BARDSLEY, W.G. : 70, 217, 1209. BARKER, C.W. : 73. BARKER, W.G. : 985. BARNA, J. : 71. BARNETT, N.M. : 72,261. BARTLlNG, Q.J. : 73. BARZ, W. : 74,97, 573. BASHOUR, N. : 384, 390. BASSIRI, A. : 75, 75a. BASTIN, M. : 76, 77, 78, 79. BATCHELOR, A.O. : 246. BATES, D.C. : 80, 198. BATES, L.S. : 980. BATRA, G.K. : 81. BAULT, A. : 82. BAUMANN, G. : 565. BAUN, L.c. : 936. BAVER, N. : 147. BAXTER, R. : 279. BAYSE, G.S. : 83, 84, 85, 907, 908, 909. BAZIN, M. : 646. BEAL, E.A. : 1049. BEARD, M.E. : 957. BECHARA, EJ.H. : 86, 228, 960, 1410. BECK, G.E. : 515a, 784. BECKMAN, C.H. : 910. BEDNAR, T.W. : 87, 88. BEEVERS, H. : 1477. BELDING, M.E. : 89. BEMILLER, J.N. : 90. BENADA, J. : 91.


BENDALL, D.S. : 1076. BENEDICT, W.G. : 92, 93. BENES, K. : 94, 502. BENITO, C : 95. BENIWAL, S.P.S. : 1341. BERA, A. K. : 206. BEREZIN, I.W. : 96, 730, 731, 732, 1358, 1359, 1361, 1362, 1466. BERGH, B.O. : 1333, 1334, 1335. BERLIN, J. : 97. BERNHARD, W. : 31. BERTAUX, B. : 333. BERVILLE, A. : 434. BESFORD, R.T. : 98. BESTER, A.I.J. : 1385, 1386, 1387. BEUTLER, E. : 47, 1167. BEWLEY, J.L. : 1274. BHARGAVA, K.S. : 99. BHARTI, S. : 99a. BHATIA, CR. : 882, 883. BHATTACHARYA, N.C : 100, 101,323,930,931,932. BHATTARCHARYA, S. : 100, 102, 103,714,911. BIDLACK, W.R. : 104. BIELER, L.Z. : 183. BIELSKI, B.H.J. : 105, 106, 107. BIEMPICA, L. : 957. BILLETT, E.E. : 1238. BIRECKA, H.: 108, 109, 110, 111,112,113,114,115,116,188. BIRKNER, M. : 482. BISWAL, V.C : n 93. BISWAS, B.B. : 1080a. BJORKSTEN, F. : 117, 118. BLAAS, J. : 156, 157. BLAICH, R. : 119. BLANC, B. : 1037. BLIGNY-FORTUNE, D. : 120, 569, 570. BLOOM, G.D. : 121, 185. BLOOMBERG, R. : 527, 1355. BLOOMGARDEN, D. : 1422. BLUM, H. : 1104. BLUME, D.E. : 122. BLUME, K.G. : 164, 1167. BLUTHNER, W.D. : 578. BLYUMENFELD, L.A. : 810. BOGDAN, S. : 123. BOISARD, J. : 1025. BOLL, W.G. : 36, 37, 38, 39, 40. BOLLER, Th. : 124. BONNER, W.D. : 1103, 1104.

259AUTHOR INDEX

BONFANTE-FASOLO, P. : 124a. BONISOLLl, F. : 125. BONZON, M. : 479. BOORSMA, D.M. : 126. BOOP, M. : 51,52, 126a, S03, S04, S05, S06, 807. BORCHERT, R. : 127, 129, J30. BORODENKO, L.1. : 10/3. BORYS, M.W. : 1294. BOS, A. : 131. BOSMAN, ET. : 132. BOTTGER, M. : [33. BOUCHET, M. : 133, 134, 135, 135a, 136,338,435,436,437,438,439,452674,851,852. BOUDET, A.M. : 20. BOUILLENNE, C. : 137. BOVERIS, A. : 138, 1103. BOWLING, A.c. : 139. BOXUS, P. : 1063. BOYER, N. : 140, 141, 142, 143, 144. BOZALIK, S.J. : 1388. BOZDECH, M.J. : 145. BRABER, J.M. : 146. BRAD, 1. : 146a, 254, 914, 1043, J223. BRADER, J.M. : 146. BRATTON, B.O. : 147, 148. BRAVINDER-BREE, S. : 1262. BREDEMEIJER, G.M.M. : 149, [50, 151, 152, 153, 154, 155, 156, 157. BREDEROO, P. : 989. BRENNAN, T. : 158. BRETON-GORIUS, J. : 159, 825. BRETTON, R. : 160. BREWBAKER, J.L. : 160a, 1010. BRIBER, K.A. : 108. BRIGHT, J.E. : 1321. BRIGNAC, Jr. P.J. : 273. BRINKMANN, F.G. : 161. BRITTAIN, M.G. : 162. BROCK-LE-HURST, E. : 362. BRODERSEN, R. : 163. BRODRICK, H.T. : 1389, 1390, 1391. ! BRONNIKOVA, T.V. : 379. BROOKS, J.L. : 696, 697. BROSS, R.J. : 164, 1167 BROUET, A. : 123. BROYKO, L.K. : 1358. BROWN, A.H.D. : 73, 165. BROWN, L.F. : 1443. BROWN, R.H. : 166 BROWNING, A. : 1062.


BRULFERT, J. : 167. BRUNNER, H. : 168. BRUNORI, M. : 1032, /033, 1123, 1441. BRYANT, S.D. : 169. BRYGIER, J. : 170. BRZOZOWSKA-HANOWER, J. : 171. BUDILOVA, E.V. : ln. BUDU, C.E. : 838. BUFLER, G. : Ina. BUGBEE, W.M. : 173. BUIS, R. : 174, 1031. BU KOVAK, M.J. : 1046, 1444. BUNT, A.H. : 194. BURG, S. : 653. BURKE, R.E. : 522. BURLESTON, B. : 1445. BURNETT, C. : 27, 175. BURR, B. : 939. BURUIANA, L.M. : 176. BUSINELLI, M. : 1307. BUTTON, J. : 177.

CABANNE, F.R. : 178. CABRILLAT, H. : 179. CACCO, G. : Il, 1251. CACHITA-COSMA, D. : 180, 181. CAIRNS, E. : 182. CAIRNS, W.L. : 182, 1381a. CALVAN, M. : 1273. CALVO, R. : 842. CAMERON, P.V. : 243. CAMMER, W. : 183. CANNON, A.M. : 184. CANNON, M.S. : 184. CAPONETTI, J.D. : 905. CAPRON, T.M. : 1427a. CARDENAS, F. : 764. CARLSON, J.A. : 632. CARLSON, P.S. : 75, 75a. CARLSOO, B. : 121, 185. CARPENA, O. : 186. CARSON, KA : 867. CARTER, D.P. : 187. CARUBELLI, R. : 1350.

AUTHORINDEX 261

CARUSO, J.L. : 19, CASADEI DE BAPTISTA, R. : 86, 228. CASHORE, W.J. : 163. CASTILLO, F. : 187a. CATALFAMO, J. L. : 108, 109, 110, 1Il, 188. CATEDRAL, F. : 189, 1181. CATESSON, A.M. : 190, 190a, 191, 192, 193,265,266. CAUBERGS, R. : 292. CAVALIERI, A.J. : 461a. CAVALIERI, E.L. : 1119. CAVATORTA, P. : 378. CECCHINI, J.P. : 871, \028. CECH, F.e. : 591. CERNOHORSKA, J. : 352. CEULEMANS, E. : 452. CHABIN, A : 646. CHADWICK, AV. : 255 CHAMPAULT, A. : 646. CHAN, H.S. : 1427a. CHAN, K.Y. : 194. CHAN, P.e. : 106. CHANCE, B. : 195. CHANDRA, G.R. : 196, 197. CHANG, e.K. : 32. CHANG, J.Y. : 197a. CHANT, S.R. : 80, 198. CHAPELLE, B. : 141. CHAPPET, A : 199, 200, 201, 202, 203, 335, 484. CHASKES, M.J. : 112. CHATTERJEE, D.K. : 204. CHATTOPADHYAY, N.e. : 206. CHATTOPADHYAY, S. : 73,205. CHAVAN, P.D. : 221. CHAUDHARY, S.S. : 723. CHAUHAN, J.S. : 207. CHAVIN, W. : 3. CHEIGNON, M. : 208. CHEN, S.L. : 209. CHERIAN, R. : 809. CHERNOFF, S. : J080. CHERRY, J.P. : 210, 211. CHERSI, A. : 1187. CHERTAL, K. : 809. CHETAL, S. : 212. CHI, E.Y. : 537. CHIANCONE. E. : 16. CHIBBAR, R.N. : 213.214,215,933. CHIGRIN, V.V. : 216.


CHILDS, R.E. : 217, 1209. CHIN, e.Z. : 218. CHIPKO, B.R. : 246. CHIRKOVA, T.V. : 219. CHMIELNICKA, J. : 220. CHOUDHARY, S.S. : 221.· CHOUREY, P.S. : 222. CHOY, Y.M. : 223, 1479. CHRISTIE, K.N. : 224, 225. CHU, M. : 225a. CHUNG, J. : 226. CHUNG, K. : 761. CHUNG, A. : 227. CHYLINSKA, K.M. : 684. CILENTO, G. : 86, 228, 350 860 960 1409, 1410, 1411, 1486. CIOPRAGA, J. : 229. CLAIRBONE, A. : 230, 231, 232. CLAIRE, A.: 140. CLAPHAM, D. : 22, 23. CLARK, H.D. : 197. CLARK, MA : 4. CLARKE, J. : 233. CLARKSON, R.B. : 591. CLEGG, M.T. : 234. CLELAND, R. : 424, 425. CLEMENTI, F. : 235. CLOCHARD, A. : 1397. CLYNE, D.H. : 236. COHEN, e. : 1422. COHEN, J.D. : 237. COHEN, Y. : 238. COHEN: ZA : 593, 1269, 1270. COLD, M.H. : 703. COLILLA, W. : 90. COLLIER, G.S. : 6. COLLIER, H.B. : 239. COLLNGS, J.R. : 240. COLLINS, N. : 166. COLLINS, T. : 1422 COLOTELO, N. : 1182. COMBATT1, N.e. : 222 COME, D. : 1320. COMSTOCK, DA : 106. CONKLIN, M.E. : 241, 1238a. CONSTABEL, F. : 242. CONTIN, G.G. : 1400. COOKE, e.T. : 243. COOMBES, AJ. : 244.

AUTHOR INDEX 263

COPES, D.L. : 245. CORBETT, M.D. : 49, 50, 246. CORIN, R.E. : 247. COSMIN, O. : 914. COTRAN, R.S. : 248, Il 16. COTTON, M.L. : 249, 250. COUDERC, H. : 342. COULOMB, P. : 251, 1347. COULSON, A.F.M. : 252. COUPE, M. : 253. COURDUROUX, J.c. : 447. COVOR, A. : 254. COX, C.D. : 247. CRAIG, M.E: : 1420. CRAKER, L.E.·: 2, 255. CRAMER-KNIJNENBURG, G. : 132. CRITCHLOW, J.E. : 256, 257, 257a. CRONENBERGER, L. : 258. CROWOEN, R.K. : 139. CSERESNYES, Z. : 506. CUNNINGHAM, B.A. : 259, 630, 733, 760, 761, 1138. CURTIS, C.R. : 260, 261, 262, 263, SOI. CZANINSKI, Y. : 192, 193,264,265,266,466. CZAPSKI, K. : 267, 268. CZARNECKA, E. : 1441.

DABROWSKA, T. : 1055. DAEMS, W.T. : 269. DA GRACA, J.U. : 269a. DALY, J.M. : 189, 270,271, 271a, 271b, 1180, 1181. DANNER, D.J. : 272, 273, 909. DARBYSHlRE, B. : 274, 275, 276. DARIMONT, E. : 277,278,279,280,281,282,283,434,437,577, 1015, 1016, 1017. DASGUPTA, P. : 102,714. DASHEK, W.V. : 284. DASS, H.C. : 285. DATTA, A.G. : 204. DAUPHIN, B. : 646. DAUSSANT, J. : 286, 287, 1124a, 1234. D'AUZAC, J. : 253. DAVIDSON, B. : 288, 937. DAVIES, D.D. : 1137. DAVIES, D.M. : 289. DAVIES, M.E. : 290. DAVIS, C. : 958.


DAVIS, L. : 973. DAVYDOV, R.M. : 810. DAVYDOVA, MA : 609. DEAL, CL. . 384, 385. DECHATELE~ R. :8TI. DEDECUE, CJ. : 130. DEEN, J.L.W. : 98. DEGN, H. : 291, 975, 975a. DE GREEF, J.A. : 292. DEGROOT, Ll. : 922. DEIMANN, W. : 293. DEJAEGERE, R. : 1139. DE JONG, D.W. : 294, 295. DEKOCK, P.c. : 296, 297. DELAIGUE, M. : 646. DELFIACCO, M. : 1114. DELINCEE, H. : 298 299 300, 301, 302, 303, 304, 305, 1068a, 1326. DELLACORTE, L. : 1188. DELRIO, I.A. : 306, 307. DEMIREVSKA-KEPOVA, K. : 55, 56, 57,308. DEMOREST, D.M. : 309, 1264, 1265. DEMORROW, J.M. : 547, 548. DENCHEVA, A.V. : 310, 311, 682. DENDSAY, J.P.S. : 312. DENNA, D.W. : 313. DENNY, P. : 553. DE OLMOS, J.S. : 314. DEPREST, B. : 1118. DE ROPP, J.S. : 724a. DE RYCKER, J. : 315, 520. DESARLO, F. : 1188. DESCHAMPS-MUDRY, M. : 200. DE SOMBRE, E.R. : 316, 317, 780, 781, 782. DESSER, R.K. : 318. DEVAY, M. : 699. DEVI, G. : 319. DEVILLERS, E.A. : 877. DEWOLF, M. : 320. DEZSI, L. : 321, 322. DHALIWAL, G. : 323. DHAWAN, A.K. : 324. DICKS, J. W. : 325. DIETRICK, W. : 320. DIJKMANS, H. : 77. DIMITRIJEVIC, L. : 326. DINELLO, R.K. : 327. DIXON, L. : 35. DJAVADI-OHANIANCE, L. : 328.

j.- •

i:

265 AUTHORINDEX

DOELLGAST, G.l. : 1318. DOLARA, P. : 1188. DOLMAN, D. : 329. DOLPHIN, D. : 327. DOMBROVSKlI, VA : 732. DONNELLAN, B. : 971. DO QUY HAl, : 330, 508. DORRIS, M.L. : 1080. DOUBEK, D.L. : 505. DOUGHERTY, H.W. : 710. DOUMENJOU, N. : 331. DOUSCHKOVA, P.1. : 310. DOUZOU, P. : 331a, 1338. DOYLE, M.P. : 332. DRAWERT, F. : 303, 304. DRESLER, S. : 1263. DREYFUS, B. : 825. DROBYSHEVA, N.1. : 1011. DROUET, A. : 1303. DUBERTRET, L. : 333. DUBIN, l. : 1415. DUBOIS, J. : 747, 748. DUBOUCHET, J. : 201, 202, 203, 334, 335, 336, 423a, 483, 484, 1058. DUBUCQ, M. : 337, 338, 440,441, 442, 674. DUDEN, R. : 339. DUFFUS, C.M. : 340. DUFFY, G. : 341. DUFFY, M.J. : 341. DUMITRESCU, M. : 342. DUMITRU, I.F. : 605. DUNFORD, H.B. : 31a, 32, 225a, 249, 250, 256, 257, 257a, 329, 343, 344, 345, 346,

347, 347a, 531,563,624,625,628,629,633,920, 920a, 928, 1069, 1120, 1121, 1122, 1268, 1275, 1276.

DUNLAP, T.W. : 1420. DUNLEAVY, J.M. : 348, 1364, 1365. 1366. DURAN, N. : 86, 228, 349, 350, 860, 960, 1409, 1410, 1411, 1486. DURAND, B. : 646, 776. DURAND, R. : 646. DURZAN, D.J. : 1073. DUTTA, S. : 67. DUVAL, J.c.c. : 351. DVORAK, M. : 352. DYM, M. : 1014. DZlEWANOWSKA, K. : 353.


EARL, J.W. : 354. EDELSTEIN, L.M. : 971, 997. EDREVA, A.M. : 355, 1127. EGAN, R.W. : 710. EGUCHI, H. : 652a. EHRENBERG, A. : 817. ELKINAWY, M. : 356. ELLIOTT, M.e. : 1429. EL-METHANY, A. : 356a. ELSTNER, E.F. : 357,489. EMANOVILOV, E. : 57. ENDERS, N.T. : 164. ENOO, T. : 358, 984, 1474. ENDRESS, A.G. : 359. ENSINK, F. T.E. : 1373. EPSTEIN, D. : 997. EPSTEIN, E. : 360. EPSTEIN, N. : 361, 1162. ERECINSKA, M. : 362. ERICKSON, S.S. : 284. ERMAN, J.E. : 252, 363. ERNEST, L.e. : 364. ESEN, A. : 365. ESQUERRE-TUGAYE, M.T. : 850. ESSNER, E. : 366, 367. ESTERBAUER, H. : 368, 369, 482. ESTERHUIZEN, E.W. : 1390, 1391. EURELL, T.E. : 184. EVANS, J.J. : 370, 371. EVANS, M.L. : 372, 373. EVANS, W.H. : 318. EVANS, R.e. : 425c. EVETT, M. : 1122

FACCIOLl, G. : 374. FAHIMI, H.D. : 293, 375, 376, 377, 558, 559, 1116, 1402. FALCIONI, G. : 1123. FAUONI, A. : 228, 349, 860, 1409. FALLOT, J. : 427. FARKAS, G.L. : 322, 729a. FARKAS, J. : 1369. FARRIMOND, J.A. : 1429. FATRAI, Z. : 1220. FAVILLA, R. : 378. FEDAK, G. : 378a.

AUTHOR INDEX

FEDKINA, V.R. : 379. FEILLET, P. : 619, 686, 688. FEINBERG, J.H. : 188. FEINGOLD, M. : 380. FEJER, O. : 699. FELBERG, N.T. : 381. FELD, R.D. : 1443. FELDER, M.R. : 382. FEL'DMAN, D.P. : 96. FENIL[, D.: 1488. FERET, P.P. : 383, 848. FERRARI, G. : 1251. FERRI, M.V. : 383a, 494. FEUCHT, W. : 1166. FEUNG, C.S. : 522. FIBIGER, H. : 1266. FIELDES, MA : 384, 385, 386, 387, 388, 389, 390, 1356, 1357. FIELDING, J.L. : 391,392, 513. FINK, B. : 393. FIORETTI, E. : 1123. FITES, R.C. : 1329, 1330. FLECHTER, RA : 18, 620, 621. FLOYD, RA : 1086. FLÜCKIGER, W. : 394, 395. FLÜCKIGER-KELLER, H. : 395. FLURKEY, W.H. : 396, 397. FOBES, J.F. : 1105, 1106, 1107. FONG, K.L. : 783. FONTAINIERE, B. : 179. FORLANI, L. : 1034. FORRENCE, L.E. : 2. FOSKET, D.E. : 1336. FOSSE, M. : 333. FOWLER, J.L. : 398, 894. FRANCALANCI, R. : J 188. FRENKEL, C. : 158, 218, 399, 400, 402, 404, 499. FRETZ, TA : 712, 713. FRETZDORFF, B. : 405. FREY, G. : 573. FRIC, F. : 406, 407, 408, 409. FRICKER, A. : 339, 995. FRIDOVICH, I. : 230, 231, 232, 532, 881. FRIEDEN, E. : 594. FRIEDHOFF, J.M. : 530. FRIEND, J. : 410. FRlES, D. : 411, 412, 413, 438, 439, 443. FRY, S.c. : 414,415. FRYDMAN, B. : 416. FRYSMAN, R.B. : 416.

267

,,.


FUCHS, W.H. : 409, 859. FUJITA. H. : 417, 663. FUJITA, S. : 418. FU KAt K. : 972. FUKUNAGA. T. : 972. FURAI, K. : 972. FUSHIKI, H. : 926.

GABORJANYI, R. : 419. GALE, M.D. : 420. GALLATI, H. : 421, 421a. GALLIANI, G. : 422. GALLIARD, T. : 423. GALLOIS, T. : 423a, 484. GALSTON, A.W. : 5, 113, 116, 665, 753, 754, 955, 956. GAMLIN, P. : 1090. GANCEVA, K. : 787. GARAY, R.V. : 782. GARBER, E.D. : 1081. GARCIA-RODRIGUEZ, M.J. : 120. GARDINER, M.G. : 424, 425. GARG, O.P. : 1204. GARRAWAY, M.O. : Ill, 114, 425a, 425b, 425c. GARRETT, J.R. : 426. GARR1S0N, L.B. : 666, 667. GAS, C. : 427. GASPAR, Th. : 133, 134, 135, 135a, 136, 137, 141, 142, 143, 144, 180, 181, 280,

281,282,283,338413,428,429,430,431,432,433,434, 435, 436, 437, 438, 439, 440, 441, 442, 443, 444, 445, 446, 447, 448, 449, 450, 451, 452, 577, 674, 749, 938, 1015, 1016, 1017, 1063, 1133, 1320, 1327, 1328, 1374, 1375.

GASYNA, Z. : 453. GAUTHIER, M.F. : 687. GEBICKI, J.M. : 107. GEELEN, J.L.M. : 1395. GEIGER, J.P. : 454, 455. GELINAS, DA : 456. GEMANT, A. : 457, 457a, GENTILE, I.A. : 458. GENTINETTA, E. : 1248, 1249. GEORGE, W.L.Jr. : 874. GEORGESCU, C.M. : 459. GEORGIEV, G.H. : 58,460,461. GEORGIEV, G.K. : 461. GETTYS, K.L. : 461a.

AUTHORINDEX 269

GEWITZ, H.S. : 462. GEYER, G. : 695. GHAZY, AM. : 650, 651. GHOSH, B. : 1185. GHOSH, J.K. : 462a. GIACOMETTI, G. : 1033. GIBSON, D.D. : 783. GIBSON, D.M. : 463,464, 767. GIBSON, Q.H. : 950. GICHNER, T. : 1302. GIEBEL, J. : 465, 1439. GILES, A.B. : 1238. GIRAUD, G. : 466. GLASIUS, E. : 1373. GOFF, c.w. : 467, 809 GOLDSTEIN, J. : 112. GOMEZ, M. : 306, 307. GONATAS, NA : 526. GONATAS, T.O. : 526. GONZALEZ-ALONZO, L.M. : 843. GOPINATHAN, K.P. : 319. GORDON, AR. : 468. GORDON, G.J. : 549. GORDON, J.c. : 469, 1447, 1453. GORDON, W.R. : 470. GOREN, R. : 442. GORENFLOT, R. : 342. GORIN, N. : 125, 471. GORZ, H.J. : 618. GOTLIEB, A : 1422. GOUJON, M. : 454, 455. GOVE, J.P. : 472, 473. GOWER, E.C. : 867. GREEN, R.C. : 474. GREGORY, L.E. : 196, 197. GREIMEL, A. : 475, 476, 477, 478. GREPPIN, H. : 135a, 187a, 282, 444, 445, 479, 658,659,660,661,749. 1015, 1016,

1017, 1018, 1019, 1020, 1021, 1022, 1023,1024, 1025, 1026. GRIFFIN, B.W. : 480, 481. GRILL, D. : 369, 482. GRISEBACH, : 507. GRISON, R. : 483, 484, 485, 1058. GROB, K. : 486. GROOME, N.P. : 487. GROSS, G.G. : 487a, 488, 488a, 489. GROSSER, C. : 1253. GROVER, Y.P. : 490. GRZELINSKA, A : 491.

PEROXIDASES 1970/1980 270

GUARNA, A. : 1188. GUHAMUKHERJEE, S. : 613, 1194, 1195, 1196, 1197, 1198. GUIBERT, B. : 46. GUPTA, B.D. : 913. GUPTA, V.K. : 9, 492, lOCH, 1340. GURUMURTl, K. : 213,214, 215, 493, 933. GURUPRASAD, K.N. : 723. GUST1N, M.K. : 962. GUZMAN, C.A. : 383a, 494, 495, 1342.

HAARD, N.F. : 402, 496, 497, 498, 499, 500, 923, 1074. HABECK, H. : 50\. HABER, A. : 106. HADACOVA, V. : 502. HADDON, L. : 503. HADLER, W.A. : 1216. HAGER, A. : 504. HAGER, L.P. : 505, 563a, 1325. HAG1MA, 1. : 13, 14, 506. HAG1WARA, T. : 604a. HAHLBROCK, K. : 507. HAl, D.Q. : 330, 508. HA1SMAN, D.R. : 509. HA1SS1G, B.E. : 510. HALDMANN, M. : 511. HALL, A. : 296. HALL, H.G. : 512. HALL, J.L. : 10,391,392,513, 5J4, 515, 593. HALL, T.C. : 515a, 784. HALLlWELL, B. : 315,516,517,518,519, 519a, 520. HALPER1N, W. : 521, 878, 879. HAM, E.A. : 710. HAMADA, G. : 971. HAMA KER, J.M. : 1245. HAMBR/CK, J.L. : 523. HAMERS, M.N. : 1433. HAM/LL, D.E. : 1239. HAM/LTON, R.H. : 522. HANCHEY, P. : 524. HANCOCK, J.f. : 461a. HANOWER, P. : 171, 524. HARGIS, J.H. : 505. HARKIN, J.M. : 525. HARPER, c.G. : 526 HARRIS, A.B. : 1351.

271AUTHOR INDEX

HARRIS, J.W. : 1191. HART, G.E. : 1164. HART, MA : 527. HARTE, C. : 1179. HARTENSTEIN, R. : 528, 529. HARTMANN, C. : 123, 1303. HASCHKE, R.H. : 194, 530. !.

HASEGAWA, Y. : 160a. HASINOFF, B.B. : 531. HASKINS, FA : 628. HASSAN, H.M. : 532. HAUN, M. : 228. HAWKINS, RA : 1027. HAYASHI, T. : 42. HAYASHI, Y. : 533, 534, 535, 1460. HAYWARD, D.M. : 284. HEGARTY, E. : 867. HEIDEMA, ET. : 471. HEINTZE, K. : 339. HEIPERTZ, R. : 1039. HELLIN, E. : 186. HEMPHILL, D.Jr. : 1467, 1468 HENDERSON, J.H.M. : 470, 536. HENDERSON, W.R. : 537, 538, 539, 540, 634.

. HENDRIKS, T. : 541. HENRIKSON, A. : 1003. HENRY, E. W. : 147, 148, 543, 544, 545 546, 547, 548, 549, 550, 551, 552, 553, 554. HENRY, Y. : 555. HEPLER, P.K. : 556, 1336. HERSZKOWICZ. 1. : 495. HERZOG, V. : 377, 557, 558, 559, 560 561, 562. HESS, C.E. : 404. HEUPEL, A.L. : 357. HEWETT, D. : 1368. HEWSON, W.D. : 346, 347, 563, 563a. HEYNE, E.G. : 259. HIDAKA, H. : 922. HIGUCHI, T. : 564, 926. HILDERSON, H.J. : 320. HILGENBERG, W. : 565. HILL, J.H. : 1366a. HILL, J.M. : 566 HIMMELHOCH, S.R. : 318. HIRAI, K. : 567. HIRANO, H. : 1471. HIROMI, K. : 900. HIRSCH, A.M. : 120, 568, 569, 570. HISLOP, E.C. : 571.


HOBNER, G. : 1253. HOBSON, G.E. : 572. HOEK. F.J. : 1143a. HOESEL, W. : 573. HOESS, R.H. : 574. HOFFEREK, K. : 575, 576. HOFFMANN, M.E. : 729b, 860. HOFFSTEIN, S. : 1422. HOFINGER, M. : 281, 577. HOHLER,B. : 578. HONlG, D.H. : 1068. HORN BROOK, K.R. : 783. HORSMAN, D.O.: 579, 580, 1427a. HORVATH, M.M. : 581. HOSHINO, Y. : 1184. HOWELL, R.K. : 262, 263. HOYLE, M.C. : 472, 473, 582 583, 584, 585, 586, 587. HRADILIK, J. : 588. HRYCAY, E.G. : 589, 590. HUANG, F.H. : 591. HUAULT, C. : 592. HUBBARD, A.L. : 593. HUBER, CT. : 594. HUBERMAN, M. : 442. HUBNER, G. : 1253. HUDEK, J. : 1277. HUISINGH, D. : 597. HUMES, J.L. : 710. HURDUC, N. : 254. HUSSEY, R.S. : 595, 596, 597.

IDA, 5. : 598, 599, 903. IIZUKA, T.c. : 678. IMAIZUMI, K. : 1206. IMASEKl, H. : 600, 1190. IMBERT, M.P. : 601, 602, 603. INKSON, R.H.E. : 296. INNOCNETI, A.M. : 604. INOUYE, J. : 604a. INSLER, V. : 380. IN1JBUSHI, T. : 899. IORDACHESCU, D. : 605. 15H11, H. : 1205. 15H11, T. : 716.

AUTHORINDEX

ISHIMARU, A. : 606. ISHIMURA, Y. : 678. IVANOVA, MA : 172. IVANOVA, N.N.: 607,6081011,1012. IVANOVA, T.M. : 609,610. IWASA, S. : 652a. IWASAKl, K. ; 716. IYANAGI, T. : 1156.

JACOBS, A.A. : 611. JACOBS, M. : 180, 181, 938. JACOBSEN, J.V. : 30. JAEGER-WUNDERER, M. : 612. JAGANNATH, D.R. ; 883. JAIN, A. : 1254. JAIN, S.K. : 1225, 1226. JAIN, S.M. : 613. JAISMAL, V. : 613a, 1115. JAMALE, B.B. : 614. JAMES, G.T.: 1291. JANKAY, P. : 615. JANKELEVICH, B.B. : 947. JANSE, C. ; 489. JANSSEN, M.G.H. : 616. JANUSKA, M. : 318. JASANI, B. ; 617 JAYASA, N.K. ; 636. JAYNES, TA : 618. JEANJEAN, M.F. ; 619. JELLINCK, P.H. : 620,621,622,668, 794, 795. JEN, J.1. : 396, 397, 1326a. JENNINGS, A.C. : 623. JENSEN, T.E. : 550, 554. JERINA, D.M. : 271b. JEVNlKAR, J.J. ; 744. JOASSIN, L. : 135. JOB, C. : 851. JOB, D. : 200, 225a, 624, 625, 626, 627, 628, 629, 1059. 1101. JOHAM, H.E. : 895. JOHN, K.V. ; 940. JOHNSON, L.B. : 630, 631. JOHNSON, MA : 632. JONARD, R. : 1043a. JONAS, D.E. : 1220.

273

i


JONES, D.G. : 243. JONES, L.R. : 1348. JONES, P. : 289, 626, 633. JONG, E.C. : 538, 634, 635. JORDAN, W. : 551. JOSEFSSON, J.O. : 779. JOSEPH, K.V. : 636. JOSH1, G.c. : 1299. JOSH1, G.V. : 614. JOSH1, M.G. : 1075. JOSH1, M.M. : 1299. JOSH1, R.D. : 99. JOUBERT, AJ. : 637. JUDEL, G.K. : 638, 639. JULAVEANU, A : 13. JULIANO, B.O. : 936, 986. JUNG, GA : 700. JUNGHANS, P. : 1253. JUNIPER, B.E. : 1117a. JUO, P.S. : 640.

KACHAR, B. : 1411 KACPERSKA-PALACZ, A : 641. KAOOUM, AM. : 1138. KAHL, G. : 642. KAHLEM, G. : 643, 644, 645, 646. KA LINER, M. : 539. KALYANARAMAN, V.S. : 647,648. KAMBOJ, R.K. : 649. KAMEL, M. Y. : 650, 651. KAMINSKI, C. : 652. KAMISAKA, S. : 1142. KANAZAWA, K. : 652a. KANG, B.G. : 653. KANG, C.H. : 941. KANG, Y.H. : 28,316. KANG, Y.J. : 654. KAOSIRI, T. : 655. KAPLAN, R. : 1422. KAPLOW, L.S. : 656. KAR, M. : 657. KARADGE, BA : 221. KARATAGLIS, S. : 1304. KAREGE, F. : 658, 659, 660, 661, 1026.

AUTHOR INDEX 275

KARNOVSKY, M.J. : 1014, 1296. 1297. KATAOKA. K. : 662,663. KATO, M. : 664. KATO, Y. : 1309. KATOH. T. : 1205. KATOMSKI, PA : 1119. KAUR, N.P. : 101,930,931. KAUR, S.P. : 816a. KAUR-SAWHNEY, R. : 665, 754. KAVANAGH, J. : 70. KAWAI, N. : 1471. KAWARDA, A. : 1300. KAY, E. : 1208, 1293. KEEN, N.T. : 996. KEENAN, EJ. : 666, 667. KEEPING. H.S. : 668. KEFELI, V. : 669. KELLER. T. : 670, 671,672. KELLY, G.J. : 673. KEMP, E.D. : 667, KENDE, H. : 124. KENNEDY, I.R. : 354. KHAN, A.A. : 439, 443, 451, 674, 1316, 1317. KHAN, M.I. : 675. KHANDUJA, S.D. : 691, 692. KHAVKIN, E.E. : 676, 1483. KHAZOVA, I.V. : 219. KHUDTAKOVA, G.M. : 607. KIDD, A. : 426. KIELISZEWSKA-ROKICKA, B. : 677. KIHARA, H. : 678. KIM, S.S. : 679, 680. KIMURA, H. : 1266. KIMURA, S. : 681. KINDL, H. : 681a. KING, C.M. : 87, 88. KIRAN, U. : 8. KITAMURA, 1. : 598, 599, 903. KITAOKA, S. : 1207. KLEBANOFF, S.J. : 89, 537, 538, 634, 635, 1122a. KLEIN, D. : 592. KLISURSKA, D.Y. : 310, 311, 682. KLUSAK, H. : 91, 683. KNAB, R. : 565. KNAPP, A.G. : 867. KNUUTTILA, M.L.E. : 1319. KNYPL, J.S. : 684. KOBREHEL, R. : 619, 685, 686, 687, 688.


KOBYL'SKAYA, G.Y. : 689. KOCH, H. : 475, 476, 477, 478. KOCHBA, J. : 360, 690, 1252. KOCHHAR, S. : 691,692. KOCHHAR, Y.K. : 691, 692, 932. KOENIGS, J.W. : 693, 694. KOHLER, B. : 695. KOKKINAKIS, D.M. : 696, 697. KOLEK, J. : 1056. KOMARYNSKY, M. : 1188. KONZE, J.R. : 697a. KOSMAN, D.J. : 1339. KOSSATZ, Y.c. : 698. KOSULINA, L.G. : 1050. KOYACS, 1 : 699. KOYACS, K. : 330, 508. KOYALEYA, L.U. : 689. KOZHANOYA,O.N. : 1126. KRASNUK, M. : 700. KRAUT, J. : 1051. KREMER, D.F. : 263. KREMER, M.L. : 701. KRENZ, J. : 465. KRINSKY, M.M. : 702. KRISNANGKURA, K. : 703 KRISPER, J. : 704. KROBER, H. : 982. KRÜGER, G. : 705. KRUGER, J. E. : 706, 707, 720, 721. KRUSBERG, L.R. : 595. KRZYWANSKI, Z. : 1294. KU, H.S. : 708, 709. KUEHL, FA : 710. KUHLMANN, W.D. : 711. KUHN, C.W. : 81. KUHNS, Ll. : 712, 713. KUMAR, A. : 613a. KUMAR, D. : 714. KUMAR, S.A. : 647, 648, 1157. KUMLIEN, A. : 121, 185, 715. KUNISHI, A.T. : 763. KURAOKA, T. : 716. KURILlNA, TA : 1359. KUTACEK, M. : 669. KUYPERS, H.G. : 717. KWIEK, S. : 718.

277 AUTHOR INDEX

LABERGE. D.E. : 706,707.719.720. 721. LACROIX. Ll. : 886. LAOONIN, V.F. : 722. LADYGINA, M.E. : 1127. LAGROU. A : 320. LAIGNELET, B. : 688. LALORAA, M.M. : 99a, 723, 855, 856, 857. LAM, TH. : 723a. LAMAISON, J.L. : 724. LA MAR, G.N. : 724a. LAMBERT, N.J. : 962. LAMOND, M. : 144. LAMPORT, D.T.A : 725, 768, 769. LANDEGREN, V. : 24. LANE, F.E. : 169. LANE, N.J. : 726. LANGOWSKA, K. : 462. LANGRY, K.C : 724a. LANIR, A : 727, 1162. LATZKO, F. : 673. LAU, O.L. : 728. LAUREMA, S. : 729. LAVANCHY, P. : 1038. LAVARENNE, A : 140. LAVEE, S. : 690, 729b, 1215. LAZAR, G. : 729a. LEAL, A : 307. LEATHER, G.R. : 2, 255. LEBEDEVA, O.V. : 730,731,732, 1359, 1360. LEE, K.C : 733, 760, 761, 1273. LEE, R.F. : 631. LEE, TT : 734,735,736, 737, 738, 739, 740, 741, 742, 743, 744. LEFF, P. : 70. LEGG, P.G. : 1452. LEGRAND, B. : 745,746,747,748,749,750, 1017, 1398. LEIGH, J.S. : 751. LENHOFF, H.M. : 943. LENNA, D. : 17. LEON, A. : 186. LEPP, N.W. : 244 LESCURE, AM. : 752, 952. LESHEM, Y. : 753, 754. LESLlE, B.A. : 1061. LEV, S.L.K. : 755. LEVER, W.F. : 971. LEVIN, S. : 380. LEVINGS, CS. : 756.


LEW, J.Y. : 757, 1208. LEWAK, S.T. : 353, 758. 1135, 1320. LEWIS, D.H. : 184. LHOSTE, A.M. : 759. LIANG, G.H. ; 259, 733. 760. 761. LIANG, Y. T. : 761. LlBERMAN-MAXE, M. ; 762. LlEBERMAN, M. : 763 .. LlEM, H.H. : 764. LlUEGREN, D.R. : 765. LlNDBECK, G. : 284. LlNSMAIER-BEDNAR, E.M. : 87, 88. LORET, C : 171. LlPETZ, J. : 766. LIS, E.K. : 1134. LITT, M. : 248. LIU, E.H.. 463, 464, 766a, ;67. 768. 769. LlVSHITZ, NA : 1199. LO, S. : 1173. LOBARZEWSKI, J. : 770, 771, 772. LOCKHART, B.E. : 773. LOEBENSTEIN, G. : 1267. LOEMOSZEWSLA-ROKICKA, B. : 774. LOEPFE, E. : 393. LOEWENBERG, J.R. : 209. LOH, J.W.C : 775. LOH, P. : 362. LOPEZ-GORGE, J. ; 306, 307. LOUIS, J.P. : 646, 776. LOUW, A. : 1396. LOW, L.E. : 611. LOY, J.B. : 777. LU, A.T. : 778. LUCK, CD. : 667. LUDDEN, P. : 271. 271a. LUNDQUISI, 1. : 779. LYLE, B.J. : 667. LYSOV, Y.P.: 1199. LYTTLE, CR. ; 317, 780, 781, 782, 976.

AUTHOR INDEX 279

MA, M. : 959. MAC CAY, P.B. : 783. MACCECCHINJ, M.L. : 783a. MACCLURE, J.W. : 122. MAC COWN, B.H. : 515a, 784. MAC COWN, D.D. : 784. MAC CREIGHT, W.H. : 785. MACDONALD, T. : 786. MACHACKOVA, 1. : 787, 788, 1487. MACHEIX, J.1. : 1043a. MACIEJEWSKA-POTAPCZYKOWA, W. : 789, 790. MACKEEVER, P.E. : 791. MACKO, V. : 792. MACLACHLAN, T. : 868. MACMILLAN, e. : 793. MACNABB, T. : 794,795. MACNICOL, PX : 796, 797. MACPHIE, J.L. : 798. MACRIS, B.J. : 799. MADER, M. : 800, 801, 802, 803, 804, 805, 806, 807, 808, 942. MAEDA, M. : 34, 904. MAGE, M. : 318. MAGEE, W.E. : 809. MAGONOW, S.N. : 810. MAGRO, P. : 17. MA1ER, R. : 811. MAILLARD, F. : 812. MAISKY, V. : 717. MAHADEVAN, S. : 647, 648. MAKINO, R. : 813, 814, 815, 816, 1454, 1460, 1460a. MALDONADO, BA : 813a. MALHOTRA, S.K. : 1247. MALHOTRA, S.S. : 1247. MALIK, e. P. : 324, 816a. MALOOF, F. : 288, 937. MALTEMPO, M.M. : 751,817. MANES, M.E. : 818. MANIGAULT, P. : 287, Il 24a. MANTLE, D. : 289. MAPSON, L.W. : 819, 820, 821. MARAITE, H. : 822. MARANI, E. : 823. MARAVOLO, N.e. : 1250. MARCHESINI, A. : 1187. MARCU, Z. : 146a, 254, 914, 1223. MARCUS, A. : 824. MARCUS, Z. : 1043. MARIE, J.P. : 825.

----


MARIGO, G. : 331. MARIGOLIASH, E. : 941. MARINESCU, M. : 229. MARKAKIS, P. : 799. MARKLUND, S. : 826, 827, 828. MARKOTAI, J. : 1129, 1130. MARKS, M.E. : 162. MARKWALDER, H.U. : 828a. MARR, e.D. : 829. MARRA, C.M. : 667. MARRUCCHINI, e. : 1307. MARSALEK, L. : 830, 831. MARSHALL, D.R. : 832, 833. MARSHALL, M. : 498. MARTE, M. : 890. MARTH, E.H : 332. MARTIN, e. : 178. MARTIN, J.e. : 505. MARTIN, S.M. : 880. MARTINEZ, J. : I043a. MARTINO, E. : 138. MARTY, F. : 834. MARTYUCHENKO, S.A. : 835. MARUYAMA, T. : 836. MASIAKOWSKI, P. : 1441. MASON, D.Y. : 837. MASSEYEFF, R. : 326. MATEESCU, MA : 838, 1163. MATHUR, S.N. : 1115. MATHYS, W. : 839. MATILE, Ph. : 486, 840. MATKOVICS, B. : 330, 508, 1220. MATKOVICS, 1. : 330, 508. MATO, M.e. : 841, 842, 843. MATSUNO, H. : 844. MATTA, A. : 458. MATTHEW, lA. : 423. MATTHEWS, P. : 845. MATTOO, A.K. : 846, 847. MAUCHAMP, J. : 1084. MAYBERRY, J.S. : 848. MAYBERRY, M. : 940. MAZAU, D. : 849, 850. MAZZA, G. : 555, 851, 852, 853, 854, 1102, 1425, 1438. McGALDRIE, T. : 1278. McGEER, E.G. : 1266. McLEESTER, R.e. : 515a. MECHAM, D.K. : 371.

i·~ ...

281 AUTHORINDEX

MEIXALF, D.G. : 7. MEERABAI, A. : 1297a. MEGHA, B.M. : 855, 856, 857. MEHTA, S.L. : 1075, 1230. MENDEZ, J. : 843, 1029. MENDGEN, K. : 858, 859. MENEGHINI, R. : 860. MENNES, A.M. : 861,862,863,979. MENZEL, D. : 864, 865. MEREDITH, W.O.S. : 721. MERRETT, M.J. : 166. MERZLYAR, M.N. : 45. MESULAM, M.M. : 866, 867. METZLER, M. : 868. MEUDT, W.J. : 869, 870. MEYER, H.E. : 522. MEYER, Y. : 804, 805. MIA, AJ. : 1073. MIASSOD, R. : 871, 1028. MICHAELS, AW. : 83. MICHELSON, A.M. : 1057. MICHOT, J.L. : 872. MIGLER, R. : 873. MIKILA, J.J. : 43. MILDVAN, AS. : 492. MILEWSKA, E. : 789. MILLER, A. : 115. MILLER, F. : 560, 561, 562. MILLER, GA : 874. MILLER, R.L. : 1282. MILLER, R.W. : 875, 876, 1233. MILLS, R.R. : 284. MILNE, D.L. : 877. MINEYEV, A.P. : 1199. MINOCHA, S.c. : 521,878,879. MISAWA, M. : 880. MISHRA, D. : 657, 998. MISRA, H.P. : 881. MITRA, R. : 882, 883. MITSUI, T. : 884. MIYOSHI, K. : 1460a. MLODZIANOWSKI, F. : 1044, 1246. MOCHAN, E. : 885, 944. MODESTO, R.R. : 236. MODI, V. V. : 846. MOHR, P. : 1091, 1092. MOLLENHAUER, H.H. : 184. MOLNAR, J.M. : 886.

PEROXIDASES 1"970/1980 282

MOLOKOV, L.G. : 887. MONAKHOVA, O.F. : 1050. MONGET, D. : 888. MONTALBINI, P. : 889, 890. MONTIES, B. : 192, 8903. MOORE, A.L. : 1103, 1104. MOORE, R.M. : 259, 733. MOORE, T.S. : 891. MOREAU, J.N. : 1397. MOREAU,M. : 193,266, 335, 336, 483, 1058. MORELL, D.S. : 893. MORFAUX, J.N. : 1397. MORGAN, P.W. : 398, 894, 895. MORIKAWA, T. : 896, MOSER, H.L.A. : 1068. MORISHIMA, 1. : 897, 898, 899, 900, 966, MORITA, H. : 876. MORITA, Y. : 598, 599, 901, 902, 903, 904, 1315, 1475. MOROT-GAUDRY, J.F. : 335,336. MORRIS, G. : 905. MORRIS, R. : 1325. MORRISON, M. : 83, 84, 85, 272, 906, 907, 908, 909, 1442. MORTON, T.C. : 540. MOSS, M.B. : 867. MUCCHIELLl, A. . 326. MUELLER, W.C. : 910. MUFSON, E.J. : 867. MUJER, C.V. : 9103. MUKHERlEE, S. : 102, 103, 911. MUKHERlI, S. : 912, 913, 999. MULLER, W.H. : 615. MULLER-EBERHARD, V. : 764. MULLIGAM, R.M. : 529. MUMFORD, L.M. : 963. MUMMA, R.O. : 522. MUNCH, P. : 806. MURESAN, T. : 914. MURPHY, C.F. : 756. MURPHY, M.J. : 915,916,917,918. MURR, D.P. : 728. MUSSELL, H.W. : 9183, 1283, 1284. MUSTACCHI, P. : 145. MYRZAEVA, S.V. : 919.

i

283AUTHOR INDEX

NADEZHDIN, A. : 920, 920a. NAOOLNY, L. : 921. h:~ NAFICHI, N.E. : 1367. ~::.:::

NAGAO, M. : 1149. NAGASAKA, A. : 922. NAGLE, D. : 1422. NAGLE, N.E. : 923. NAINAWATEE, H.S. : 212, 649. NAIK, M.S. : 1153. NAITO, N. : 1458. NAKAGAWA, H. : 969. NAKAI, Y. : 663. NAKAJlMA, R. : 924, 925, 1460a, 1463. NAKAMURA, C. : 288. NAKAMURA, Y. : 926. NAKANISHI, S. : 927. NAKANO, Y. : 1207. NAKATANI, H. : 900, 928. NANDA, J.S. : 207. NANDA, K.K. : 100, 101,213,214,215,323,493,930,931,932,933, 1157. NANDI, B. : 206. NANDRIS, D. : 455. NASINEC, V. : 788. NASSIF-MAKKI, H. : 242. NATARELLA, N. : 934,935. NAVASERO, E.P. : 936. NEARY, J.T. : 288, 937. NEGRUTlU, I.: 180, 181,938. NELSON, E.C. : 939, 940, 941. NEMCSOK, J. : 581. NESSEL, A. : 807, 942. NEUCERE, N.J. : 1322. NEUHAUSSER, E.F. : 529. NEUKOM, H. : 828a. NEUMANN, H. : 360 NEWCOMB, A.M. : 622. NEWCOMB, W. : 653. NEWELL, PA : 329. NGO, T.T. : 943. NICHOL, A.W. : 893. NICHOLlS, P. : 885. NICHOLLS, P. : 944. NICOLAE, S. : 15. NICULESCU, S. : 229, 605. NIEDERMEYER, W. : 945. NIEMTUR, S.T. : 946. NIKAIDO, H. : 599. NIKOLAEVA, M.G. : 947. NIKOLOV, S. : 948.


NIR. 1. : 949. NISH1YAMA. F. : 1471. NOBLE. R.W. : 950. NOGUCHI, M. : 1210. 121 J. 1212. NORMAN, T. : 25. NORRIS. S.H. : 236. NORTHCOTE. D.H. : 503. 1478. NORTON. W.T. : 183. NOUGAREDE. A. : 951. 952. NOVACKY. A. : 953, 954. NOVAK. J.F. : 955, 956. NOVIKOFF, A.B. : 957, 958, 959. NOVIKOFF, P.M. : 958, 959. NOVITSKI, M. : 164. NUMEZ, J. : 872, 1412.

O'BRIEN, C.R. : 960. O'BRIEN, J.S. : 1039. O'BRIEN, P.J. : 474, 589, 590, 960, 961, 1035, 1308. O'BRIEN, T.P. : 1241. OBST, Y.R. : 525. OCHIAI, H. : 1205. OCKERSE, R. : 962, 963, 964. O'CONNOR, M.N. : 548. ODAJIMA, T. : 965. ODOARDI, M. : 987, 1248, 1249. OERTLI, J.J. : 395. OGAWA, S. : 897, 898, 899, 900, 966. OGISO, K. : 1301. O'HEOCHA, C. : 915, 916, 917, 918. OHGUCHI, T. : 967. OHKAWA, K.I. : 31, 970. OHLSSON, P.J. : 220, 751, 817, 828, 968, 1002, 1003, 1004. OHRMAN, B..: 1005. OHTAKl, S. : 969. OKA, H.I. : 984. OKUN, M.R. : 971, 997,1132. OKUNO, Y. : 972. OLIVEIRA, O.M. : 86, 228. OLSEN, J.L. : 973. OLSEN, L.F. : 974, 975, 975a. OLSEN, R.L. : 976. OLSON, A. : 976a. OLTEANU, G. : 459. OMRAN, R.G. : 977.

k>l',':....

285 AUTHORINDEX

ONG, H. T. : 978. OOSTROM, H. : 863, 979. OPARA, A. : 828. ORTEGA, E.I. : 980. OSBORNE, D.J. : 981,1108,1109,1110,1154,1155. OSHINO, N. : 362. OSSELTON, J.e. : 823, 1111. OSTY, J. : 872. OR, N. : 971. ORY, R.L. : 210, 211. OVCHARENKO, GA : 607, 1012. OZEL, M. : 982.

PADMA, A. : 983. PAl, e. : 984. PALFI, G. : 322. PALMER, e.E. : 985. PALMIANO, E.P. : 986. PALMIERI, S. : 987. PANDEY, R.L. : 490, PANTEL, S. : 988. PAPADIMITRIOU, J.M. : 989, 1117. PARISH, R.W. : 990, 991, 992, 993, 994. PARK, K.H. : 995. PARTRIDGE, J.E. : 996. PARUPS, E.V. : 875. PASMAN, A.J. : 1143a. PATEL, e.S. : 536. PATEL, R.P. : 997, 1132. PATEL, V. : 273. PATRA, H.K. : 998. PATRIARCA, P.e. : 998a. PAUL, A.K. : 999. PAUL, B.B. : 611,1000,1001. PAUL, K.G. : 220, 751, 817,828,968, 1002, 1003, 1004, 1005, 1006. PAULSEN, G.M. : 733. PAULUS, K. : 339. PAWAR, V.S. : 1007. PAYNE, M.G. : 1079. PEDERSEN, M. : 1009. PEIRCE, L.e. : 1010. PElVE, Y.V. : 608, 1011, 1012, 1013. PELLINIEMI, L.J. : 1014. PENEL, CI. : 135a, 282, 444, 445, 479, 658, 659, 660, 661, 749,1015, 1016, 1017,

1018, 1019, 1021, 1022, 1023, 1024, 1025, 1026.


PENNEY, G.O. : 1027. PENON, P. : 871, 1028. PEREIRA, J.R. : 1029. PERESSE, M. : 193, 423a, 266, 484. PEREZ DE LA VEGA, M. : 95. PERL, M. : 1096, 1097. PERLEY, J.E. : 785. PESCE, AY. : 236. PESCI, P. : 1400. PETCULESCU, : 176. PETER, R.. : 553. PETERSSON, L. : 817. PETZOLD, H. : 982. PFE1L, E. : 705. PFLUG, W. : 1029a. PHAN, C.T. : 1030. PHELPS, C. : 1032, 1033, 1034. PHILLlPS, D.R. : 423. PHlPPS, DA : 244. PHIPPS, J. : 174, 1034. PIATT, J. : 1035. PICKERING, J.W. : 1036, 1054. PIEFKE, J. : 462. PILET, P.E. : 485, 742, 812, 1037, 1038. PILZ, H. : 1039. PINCKARD, JA : 1417. PINCUS, S.H. : 1040. PINGEL, U. : 1041. PINO, R.M. : 1042. PIRRWITZ, J. : 1092. PIRVU, T. : 146a, 1043. PITTS, A : 1421. PLACHY, C. : 1176. PLAPINGER, R.E. : 1184. POËSSEL, J.L. : 1043a. POH-FlTZPATRICK, M.B. : 764. POLEVOl, V.V. : 689. POLlTYCKA, B. : 1044. POLLAK, V.E. : 236. POMMIER, J. : 1412. POOVAIAH, B.W. : 1045, 1046, 1047, 1048. POPOV, D. : 13. PORTSMOUTH, D. : 1049. POTAPOV, N.G. : 1050. POTTY, V.P. : 636. POU LOS, T.L. : 1051. POURRAT, A : 724. POURRAT, H. : 724. POUX, N. : 1052, 1053.

287 AUTHOR INDEX

POWELL, B.L. : 1036, 1054. PRASAD, R. : 1200. PRASAD, S. : 1247. PRATT, H.K. : 708, 709. PRATT, J.M. : 6. PRETLOW, T.G. : 162, 1421. PRETORIUS, W.J. : 1392. PRONINA, N.B. : 722. PRZYBYLSKA, J. : 1055. PSENAKOVA, T. : 1056. PUCHALSKI, J. : 1144, 1145. PUFF, C. : 704. PUGET, K. : 1057, PUGIN, A. : 336, 423a, 1058. PUJARNISCLE, S. : 253. PULITI, R. : 1188. PULLMAN, H. : 1345. PUPPO, A. : 1059. PUROHIT, S.D. : 1060, 1060a, 1060b, lO73a, 1073b. PUTNEY, J.W. : 1061. PUXEDDU, P. : 1114.

QUAIL, P. : 1062. QUALSET, C.O. : 1226. QUINANA, N. : 957, 958, 959. QUOIRIN, M. : 1063.

RAA, J. : 356, 1064, 1065, 1066, 1067. RACKIS, J.J. : 1068. RADOLA, B.J. : 298, 299, 300, 301, 302, 303, 304, 1068a, 1131. RAHlMTULA, A.D. : 961. RAJHATHY, T. : 378a. RAKADJIEVA, D.L : 58a. RALSTON, J. : 1069. RAM, C. : 59, 60, 61, 62, 1070, 1071, 1072. RAMAIAH, P.K. : 1073. RAMAKRISHNAN, T. : 319. RAMAWAT, K.G. : 1060, 1060a, 1060b, lO73a, 1073b. RAMAZANOVA, L.K. : 1298. RAMSEY, E.E. : 667. RAMIREZ, DA : 910a.


RANADIVE. A.S. : 1074. RANJEVA. R. : 20. RANSON, RJ. : 1441. RAO. S.S. : 1189. RAO, V.R. : 1075. RAPPAPORT, L. : 1075a. RASMUSSEN, L.F. : 163, 1045, 1046, 1047. RATHMELL, W.G. : 1076, 1077, 1078. RAUF, A. : 1078a. RAUTELA, G.S. : /079. RAWITCH, A.B. : 1080. RAY, CG. : 89. RAY, K. : 1080a. RAY, P.M. : 373 RAYCHEBA, J. : 250. REBAGAY, G.R. : 1203. RECHTORIS, C : 1284. REDDY, G.M. : 983. REDDY, K.B.S.M. : 1279. REDDY, M.M. ; 1081, 1082, 1083. REGARD, E. : 1084. REID, R. : 940. REIGH, D.L. : 35, 1085, 1086, 1087, 1088. REIMANN, L. : 1089. REINER, A. : J090. RENNERBERG, R. : 1091, 1092. RENNERT, A. : 789. RENNKE, H.G. : 1093. RENWICK, J.A.A. : 792. RETHORE, J.L. : 427. RETIG, N. : 1094, 1095. REUVENI, R. : 1096, 1097. REYNOLDS, T. : 1098. RHODES, J.M. : 1099. RICARD, J.R. : 627, 628, 629, 852, 871, 1028, 1059, 1101, 1102,1438. RICE, R.M. : 556. RICH, P.R. : 1103, 1104. RICHARD, L.B. : 547, 548, 552. RICK, CM. : 1105, 1106, 1107. RIDGE, 1. : 981, 1108, 1109, 1110. RIETVELD, W.J. : 823, 1111. RIGAUD, J. : 1059. RINOONE, B. : 421a, 422. RINEHART, R. : 35. RITZERT, R.W. : 1113. RIVA, A. : 1114. RIZVI, S.J.H. : 1115. ROBBINS, D. : 1116. ROBERTSON, B. : 1067.

AUTHORINDEX 289

ROBERTSON, JA : 1117. ROBINS, R.J. : 1117a. ROCK, G.L. : 743. RODRIGUEZ-KABANA, R. : 1348. ROE, C.H. : 674. ROELS, F. : 1118. ROGAN, E.G. : 1119. ROMAN, R. : 1120, 1121, 1122. ROMER, D. : 459. ROOS, D. : 131,269. ROSEN, H.·: 1122a. ROSENSTOCK, G. : 1484, 1485. ROSHCHUPKlNA, T.G. : 607. ROSS, AF. : 1221, 1222. ROSS, D. : 1433. ROTH, R.W. : 1119. ROTTLlO, G. : 1123. ROUGE, P. : 1124. ROUSSAUX, J. : 287, 1124a. ROUTLEY, D.G. : 587. ROZHKOVA, G.D. : 1358, 1361, 1362. RUBERY, P.H. : 1125. RUBIN, BA : 45,172,609,1126,1127,1128. RUCHEL, R. : 175. RUCKER, W. : 1129, 1130, 1131. RUCKPAUL, K. : 1092. RUDICH, J. : 1095. RUDIN, Y. : 328, 783a. RULE, AJ. : 1132. RUNKOVA, L.V. : 1133, 1134. RUSSO, J.F. :147. RYAN, J.N. : 1446. RYCHTER, A : 158, 758, 1135. RZUCIDLO, L. : 718.

SACHAR, R.C. : 312, 1315. SACHER, JA : 1136, 1137. SACKSTON, W.E. : 238. SADANAGA, K. : 1469, 1470. SADANANDAM, A : 1297a. SAE, S.W. : 1138. SAFONOV, V. : 1139. SAFONOVA, M. : 1139. SAGI, F. : 419. SAGIV, J. : 1140.


SAHULKA, J : 1141. SAIGO, S. : 678. SAlTO, K. : 1235. SAKURAI, N. : 1142. SALAMINI, F. ; 987, 1248, 1249. SALVATERRA, P.M. ; 1235. SAMMONS, R. : 837. SAMSHERY, R. ; 1143. SANDERS, G.T.B. : 1143a. SANIEWSKI, M. ; 1144, 1145, 1482. SANO, H. : 1146, 1147, 1148, 1149. SANO, T. : 900. SANTIMONE, M. ; 1150, 1151, 1152. SANTOS, S. : 164. SARDHAMBAL, R.V. : 1153. SARGENT, J.A. : 981, 1154, 1155. SARKISSIAN, M.U. : 1164. SARMA, TA ; 8. SARRIS, J. ; 1397. SASSER, J.N. ; 596, 597. SAULESCU, N.N. : 14. SAUTICH, MA : 216. SAVAGE, N. : 240. SAWADA, Y. : 1156. SAWANO, F. ; 417. SAWHNEY, N. ; 1157. SAWHNEY, S.S. : 1157. SBARRA, A.J. : 611, 1000, 1001. SCALLA, R. : 178. SCANDALIOS, J.G. : 30, 1158, 1159. SCANNERINI, S. : 124a. SCARPONI, L. : 1307. SCHAEFER, H. : 1160. SCHAEVERBEKE, J. : 208. SCHAFER, P. : 1161. SCHAFER, W. : 305. SCHATZ, G. : 328, 783a. SCHAUMBORG-LEVER, G. : 1132. SCHE1D, B. : 957. SCHEJTER, A. : 361, 727, 1[62. SCHELL, H.D. ; 838, 1163. SCHELLER, F. : 1091, 1092. SCHERTZ, K.F. : 1164. SCHIPPER, Jr. A.L. : 510, 1165. SCHLEGEL, R. : 578. SCHLOSS, P. : 808. SCHMID, P.P.S. ; 1166. SCHMIDT, G.M. ; 164, 1167. SCHMIDT, H. : 1168.

AUTHOR INDEX 291

SCHMIDT-ULLRICH, B.: 1132. SCHNEIDER, E.A. : 1169 SCHNEIDER, J. : 1170 SCHOKNECHT, J. : 809. SCHONBAUM, G.R. : 492, 1089, 1172, 1173, 1427. SCHOPFER, P. : 1174, II 74a, 1175, 1176. SCHREIBER, W. : 1177, 1178. SCHROEDER, W.A. : 197a. SCHULTZ, J. : 381. SCHULZ, H. : II 78a. SCHUPPER, H. : 51 1. SCHWACHHOFER, K. : 136,283.. SCHWAGER, H. : 672. SCHWARZL, E. : 368. SCHWENZER-RODRIGUEZ, N. : 1179. SCHWIND, F. : 135. SCOTT, K.M. : 1027. SEEVERS, P.M. : 271, 271a, 1180, 1181. SEIDLOVA, F. : 94. SEKHON, A.S. : 1182. SELIGMAN, A.M. : 949, 1183, 1184. SELL, H.M. : 1467, 1468. SELS, A.A. : 170. SELVARAJ, RJ. : 1000, 1001. SEMANCIK, J.S. : 773. SEMENOVA, MA : 172. SEN, S.P. : 103, 462a, 1184a. SENGUPTA, B. : 1184a. SENGUPTA, D.N. : 462a, 1184a. SENGUPTA, T. : 1185. SEQUEIRA, L. : 921, 1077, 1078, 1186. SEQUI, P. : 1187. SERY, T. : 511. SESSA, D.J. : 1068. SEVERSON, Jr. J.G. : 775. SEVHONKIAN, S. : 1038. SEVIER, E.D. : 1187a. SEXTON, R. : 514, 515. SGARAGLI, G. : 1188. SHAILA, M.S. : 319. SHANKARLINGAM, T. : 1189. SHANNON, L.M. : 233, 757, 1187a, 1190, 1208, 1293. SHANNON, M.C. : 1191. SHANNON, S. : 1192. SHANNON, Jr. W.A. : 1184. SHAPIRO, B.L. : 26. SHARMA, R. : 1193, 1194, 1195, 1196, 1197, 1198. SHARMA, S.c. : 499. SHARMA, V.K. : 490.


SHARONOV, Y.A. : 810, 1199. SHARONOVA, NA : 1199. SHAW, C.R. : 1200. SHAW, G. : 1278. SHEEN, S.J. : 1201, 1202, 1203. SHEID, B. : 957. SHELTON, E. : 318. SHEORAN, T.S. : 1204. SHERI F, M. : 356a. SHERWOOD, R.T. : 1370, 1371. SHIBATA, H. : 1205. SHIBATA, K. : 1142. SHIGA, 1. : 1206. SHIGEOKA, S. : 1207. SHIH, J.H.C. : 1208. SHIH, L.M. : 116, 754. SHIMIZU, Y : 1409, 1486. SHIN, W.Y. : 959. SHINDLER, J.S. : 1209. SHINSHI, H. : 1210, 1211, 1212. SHIRINSKAYA, M.G. : 1012. SHIRO, Y. : 966. SHIV-PRAKASH, : 1153. SHUMAKER, K.M. : 1213. SHUSTERMAN, D. : 163. SHUTOVA, E.A. : 216. SIEGEL, B.Z. : 1214, 1215, 1273. SIEGEL, S.M. : 1214, 1215, 1273, 1415. SIES, H. : 562. SILVEIRA, S.R. : 1216. SILVERTEIN, R.M. : 505. SIMOLA, L.K. : 1217, 1218, 1219. SIMON, L.M. : 1220. SIMONS, T.J. : 1221, 1222. SINDILE, N. : 1223. SINGH, D. : 1227, 1228, 1229. SINGH, J.P. : 1153, 1224. SINGH, M.P. : 1230. SINGH, R.S. : 1225, 1226, 1227, 1228, 1229. SINGH, T.G. : 1189. SINGH, Y.D. : 99a. SINGHAL, N.e. : 1230. SINI(, Jr. K.e. : 934, 935, 1428. SIRCAR, S.M. : 1185. SIRJU, G. : 1231. SIRKAR, S. : 1232. SIROIS, J.e.L. : 876, 1233. SITZMAN, E.V. : 941. SKAKOUN, A. : 1234.

AUTHORINDEX 293

SLEMMON, J.R. : 1235. SMAOUI, A. : 1236. SMILLIE, L.B. : 1426, 1427. SMINIA, T. : 161. SMITH, D. : 446. SMITH, E.C. : 679, 680, 755, 1036, l054, 1085, 1087, 1088, 1161. SMITH, G.W. : 188. SMITH, H. : 1237. SMITH, H.H. : 222, 241, 574, 786, 1238, 1238a, 1239 SMITH, K.M. : 724a, 1240. SMITH, M.D. : 809. SMITH, M.H. : 1241. SMITH, P.1. : 1242. SMITH, R.L. : 1243, 1244. SNYDER, E.B. : 1245. SOBKOWIAK, A. : 1246. SOKOLOVSKA, YA : 219. SOLHEIM, B. : 1067. SOLOMOS, T. : 1247. SOLTANI, M.H. : 1402. SOOBACK, M. : 288. SOOST, R.K. : 365. SOPANEN, T. : 1218, 1219. SOPORY, S.K. : 613, 1194, 1195, 1196, 1197, 1198. SORENSON, J.c. : 1159. SORESSI, G.P. : 987, 1248, 1249. SPAETH, S.c. : 1250. SPENCER, D. : 420. SPENCER, M. : 1247. SPETTOLI, P. : Il, 1251. SPICER, S.S. : 791, 1282. SPIEGEL-ROY, P. : 177, 690, 1252. SPIKES, J.D. : 654. SPISUPALUCK, S. : 972. SPRINZ, H. : 1253. SPROOL, J. : 795. SRIDHAR, R. : 1253a. SRIVASTAVA, G.P. : 99. SRIVASTAVA, H.S. : 1254. SRIVASTAVA, K. : 47. SRIVASTAVA, O.P. : 1255, 1256, 1257, 1258, 1259. STAEHELlN, A. : 187. STAFFORD, HA : 1260, 1261, 1262, 1263. STAHMANN, MA : 309, 571, 1082, 1083, 1264, 1265. STAINES, WA : 1266. STARK, J.M. : 617. STARRATT, A.N. : 744. STASINOS, S. : 1279. STECHER, K.J. : 870.

PEROXIDASES 1970/1980 294

STEELINK, C : 1476. STE1GLEDER, G.K. : 1345. STEIN, A. : 1267. STEINER, H. : 347, 1268. STEINMAN, RM. : 1269, 1270. STEPHAN, D. : 1271. STEPHENS, G.J. : 1272. STEVENS, H.C': 1273. STEWART, P.R. : 1437. STEWART, R.R.C : 1274. STIEBER, A. : 526. STIGBRAND, T. : 220, 1006. STILLMAN, J.S. : 347a, 1275, 1276. STILLMAN, M.J. : 1275, 1276. STOESSL, A. : 743, 744. STONIER, T. : 480, 1277, 1278, 1279, 1280, 1281. STOPPANI, A.O.M. : 138. STOTZKY, G. : 640. STOWARD, P.J. : 224,225, 1282. STOWELL, CP. : 574. STRAND, L.L. : 1283, 1284. STRAUS, W. : 1285, 1286, 1287, 1288, 1289, 1290. STRAUSS, R.R. : 611, 1001. STRAUVEN, TA : 1295. STREEFIŒRK, J.G. : 126, 989, 1292. STREET, H.E. : 623. STR1CKLAND, E. : 1293. STROINSKl, A. : 1294. STROUT, H.V. : 288, 937. STRUM, J.M. : 1295, 1296, 1297. STUART, M. : 1086. STUBER, CW. : 756. SUAREZ, S.J. : 359. SUBHASH, K. : 1297a. SUDERSHAN, : 8. SUGAI, N, : 970. SUKHORZHEVSKA1A, T.B. : 676. SULEIMANOU, \.G. : 1298. SUMPTER, NA : 1164. SUTER1, B.D. : 1299. SUZUK1, Y. : \300, 1301. SVACHULOVA, J. : 1302. SWAMY, G.K. : 1297a. SWAN, GA : 1242. SVRKOTA, B. : 1303. SYMEONIDIS, L. : 1304. SYONO, K. : 1305. SYREN, E. : 1306. SZWEYKOWSKA, A. : 1170, 1246.

AUTHOR INDEX

TAFURI, F. : 1307. TAKAHASHI, M. : 41. TAKANAKA, K. : /308. TAKEO, T. : 1309. TALWAR, S. : 613. TAMURA, M. : /310, 1311, 1312, 1460a. TAMURA, Y. : 1313. TANAKA, S. : 31, 970. TANAKA, Y. : 1314. TANEJA, S.R. : 1315. TANI, T. : 1458. TAO, K.L. : 1316, 1317. TARASEVICH, M.R. : 1465. TAUROO, A. : 1080. TAVASSOL/, M. : 764. TAYLOR, D.D. : 1318. TAYLOR, D.M. : 895. TAYLOR, I.E.P. : J349. TAYLOR,O.C. : 359. TAYLOR, S.A. : 1357. TEISSERE, M. : 871, 1028. TENOVUO, J. : 1319. TEPPAZ-MISSON, C. : 447. TERNYNCK, T. : 160. TERRANOVA, WA : 556. TESTA-RIVA, F. : 1114. TEWARI, M.N. : 59, 60, 61, 62, 63, 64, 65, 66, 1070, 1071, 1072. THEVENOT, C. : 1320. THIRUPATHAIAH, V. : 1189. THOMPSON, K.R. : 1239. THOMAS, D.L. : 69, 1321, 1322. THOMAS, E.L. : 44, 1323, 1324. THOMAS, JA : J325. THOMAS, P. : 1326. THOMAS, R.L. : 1326a. THORNTON, J.D.. 410. THORPE, TA : /34,446, 448, 1327, 1328. THURLOW, M.D. : 329. TING, P.L. : 481. T1NGEY, D.T. : 1329, 1330. T1RIMANA, A.S.L. : 1331. T1XIER-VIDAL, A. : 1337. TOBIN, c.L. : 500. TODD, M.M. : 1332. TOKUMASUS, : 664. TOMARO, M.L. : 416. TOMASZEWSKI, M. : 1134. TONO, T. :418. TORRES, A.M. : 1333, 1334, 1335.

; .

295 1

..


TORREY, J.c. : 1336. TOUGARD, C. : 1337. TOURAINE, R. : 333. TOWERS, G.J.N. : 1137. TOWILL, L.R. : 209. TRANTALIS, J. : 28. TRAN THAN VAN, M. : 445, 448, 1328, 1345. TRAVERS, F. : 1338. THEHERNE, J.E. : 726. TRESSEL, P. : 1339. TREURNIET, F.E. : 863, 979 TRIPATHI, R.K. : 570, 1340, 1341. TRIPPI, V.S. : 167,494, 1342, 1343, 1344, 1481. TROJANOWSKI, J. : 772. TRONSMO, A. : 1067. TROST, T.H. : 1345. TRUCHET, G. : 1346, 1347. TRUELOVE, B. : 1348. TSAY, R.C. : 1349. TSEKOS, 1. : 1304. TSIKOV, D. : 948. TSUJI, A. : 34. TU RCON, G. : 1382. TURCU, A. : 1163. TURIN, BA : 1113. TURNER, P.T. : 1351. TUTSCHEK, R. : 1352. TYSON, H. : 384, 385, 386, 387, 388, 389, 390, 527, 1353, 1354, 1355, 1356, 1357.

UDA, H. : 836. UEMOTO, S.c. : 652a. UGAROVA, N.N. : 29,96, 730, 731, 732, 1358,1359, 1360, 1361, 1362. ULIASZ, M. : 641. UNGEMACH, J. : 808. UNLUER, 0 : 78, 79. URBAN, P. : 110. URBANEK, H. : 790. URITANI, 1. : 844, 1190, 1314, 1363, 1363a. URS, N.V.R. : 348, 1364, 1365, 1366, 1366a.

1

AUTHORINDEX 297

VACCA, L.L. : 1367, 1368. VACKOVA, K. : 669. ~~~t~VALDüVINOS, J.G. : 363, 554. VAMOSVIGYAZO, L. : 1369. VAN BERGEN-HENEGOUW, J. : 132. VANBERKEL, T.J.C : 269. VANCE, CP. : 1370, 1371. VANDERMAST, CA. : 1372. VANDERMEULEN, J. : 1118. VAN DER PLOEG, M. : 1292. VANDERRHEE, H.T. : 269. VANDESTOUWE, R. : 1277. VAN DE WALLE, CM. : 1061. VANDUIJN, P. : 989. VAN HAERINGEN, N.J. : 1373. VAN HOOF, P. : 441,449, 1374, 1375. VAN HOOF, R. : 292. VAN HUYSTEE, R.B. : 182, 698, 813a, 1255, 1256, 1257, 1258, 1259, 1271, 1376,

1377, 1378, 1379, 1380, 1381, 1381a, 1382, 1403, 1404. VANINGEN, E.M. : 11p. VAN LELYVELD, U. : 269a, 637, 877, 1383, 1384, 1385, 1386, 1387, 1388, 1389,

1390, 1391, 1392. VAN LOON, L.C : 1393, 1394, 1395. VAN ZYL, A. : 1396. VARDI, A. : 177. VARFOLOMEEV, S.D. : 1465, 1466. VARNER, J.E. : 30. VAROQUAUX, P. : 1397. VASILEVA, A.V. : 610. VASIL'EVA, T.E. : 1362. VASSEUR, J. : 750, 1398. VAUGHAN, D. : 297. VEECH, J.A. : 1399. VEGETTI, G. : 1400. VELAN, B. : 51 \. VELEMINSKY, J. : 1302. VENERE, R.J. : 140\. VENKATACHALAM, MA : 1093, 1402. VENNESLAND, B. : 642. VER BEEK, R. : 413, 450, 451. VERMA, D.P.S. : 1403, 1404. VERMA, M.N. : 1340. VERNANT, J.P. : 825.

. VERWOERD, N. : 1111. VEST, G. : 1047. VETTER, J. : 1405, 1406, 1407. VICKERY, R.S. : 847, 1408.


VlDIGAL, c.c.c. : 228, 350, 1409, 1410, 1486. VlDIGAL-MARTINELLl, C. : 1411. VIGIL, E.L. : 1332. VILLIERS, EA : 877. VIRION, A. : 1412.

, VIRON, A. : 711. VOHRA, K. : 1341. VORA, A.B. : 1413, 1414. VORONKOV, L.A. : 1128. VORONOVA, VA : 29. VYAS, A.V. : 1414.

WABER, J. : 964, 1415. WAHID, M. : 1416. WAIGHT, R.D. : 70. WAKS, M. : 16. WALTERS, M.N.1. : 1117. WANG, S.c. : 1417. WARDALE, DA : 820, 821, 1418. WATANABE, T. : 1419. WEAVER, EA : 1239. WEAVER, G.M. : 285. WEBSTER, B.T. : 1420. WEENING, R.S. : 1433. WEIL, H.R. : 1345. WEIR, E.E. : 1421. WEISSMANN, G. : 1422. WEISZ, H. : 988. WELlNDER, K.G. : 853, 854, 1423, 1424, 1424a, 1425, 1426, 1427. WELLBURN, A.R. : 579, 580, 1427a. WELSH, H. : 553. WENDER, S.H. : 679, 680, 755, 1036, 1054, 1087, 1088, 1161. WENNBERG, R.P. : 163. WERNER, D.J. : 1428. WESTON, G.D. : 1429. WETTSTEIJN, E.A. : 1430. WEVER, R. : 131, 1433. WHEELER, H. : 953, 954. WHITAKER, D.R. : 778. WHITMORE, F.W. : 1434, 1435, 1436, 1436a. WICKLlFF, C. : 1329, 1330. WIEBE, H.H. : 1048. WIEGAND, N.K. : 1104. WIGHTMAN, F. : 1169.

AUTHOR INDEX . 299

WILLIAMS, B.J. : 1415. WILLIAMS, E.E. : 1421. WILLIAMS, H. : 845. WILLIAMS, P.G. : 1437. WILLIAMS, R.J.P. : 1102, 1438. WILSKI, A. : 465, 1439. WILSON, J.M. : 1440, 1448, 1449. WILSON, L.A. : 601, 602, 603, 1231. WILSON, M.T. : 1441. WISE,B. : 1442. WISSE, E. : 1118. WITHAM, F.H. : 700. WITTE, D.L : 1443. WITTENBACH, VA : 1444. WOCHOR, Z.S. : 1445. WOESSNER, J.F. : 1446. WOJCŒCHOWSKI, J. : 1294. WOLFE, R. : 499. WOLFFGANG, H. : 576. WOLTER, K.E. : 1447. WONG, E. : 1440, 1448, 1449. WONG, Y.S. : 223, 1479. WOOD, J.L. : 226. WOOD, K.R. : 68, 1272, 1450, 1451. WOOD, R.L : 1452. WOODSON, G. : 1368. WOOLTORTON, L.S.c. . 1099. WORLEY, J.F. : 196, 197. WOZNY, A. : 1044. WRAY, P.H. : 1453. WRIGHT, P.E. : 1438. WRIGHT, R.D. : 70. WYLER, R. : 393. WYNDALE, R. : 452. WYMAN, J. : 16. WYSZOMIRSKA, J. : 718

YAKOVLEV, B.V. : 887. YAMADA, H. : 533,813, 1454, 1455, 1456, 1460. YAMAGUSHI, T. : 1457. YAMASHITA, Y. : 1457. YAMAMOTO, H.. 1458, 1474a. YAMAZAKI, H. : 1461, 1463. YAMAZAKI, I. : 33, 533, 534, 535, 606, 681, 813, 814, 815, 816,924,925,965,969,

1156, 1312,1454, 1455, 1456, 1459, 1460, 1460a, 1461, 1462, 1463, 1472.


YANEZ. J. : 307. YANG, H.M. : 1277, 1280, 1281. YANG. S.F.. 708. 709, 728, 1464. YAROPOLOV, A.1. : 1465, 1466. YASUNAGA, T. : 900 YEH. R. : 1467, 1468. YEN. S.T. : 1469, 1470. YOKOTA. K.N. : 1462, 1463, 1472. YOKOYAMA, M. : 836, 1471. YONEDA, Y. : 1473, 1474. YONETANI, T. : 252, 363, 1311, 1474a. YONEZAWA, T. : 899,900. YOSHIDA, C. : 902, 903, 904, 1475. YOUNG, L.W. : 397. YOUNG, M. : 1476. YOUNG, 0 : 1477. YOUSSEF, A.A. : 356a. YUNG, K.H.. 223, 1478, 1479.

ZAAR, K. : 1480. ZADEK, H.E. : 1344, 1481. ZALEWSKA, J. : 790, 1482. ZARSKA-MACIEJEWSKA, B. : 758. ZEBA, B. : 1059. ZELENEVA, I.V. : 1483. ZENTMYER, GA : 655. ZHIVOPISTSEVA, I.V. : 1128. ZHIZNEVSKAYA, G.Y. : 1013. ZHURKlN, V.B. : 1199. ZIMMERMANN, H.J. : 1484, 1485. ZIMNIAK-PRZYBYLSKA, Z. : 1055. ZINNER, K. : 228, 350, 1409, 1410, 1411, 1486. ZMRHAL, Z. : 787, 788, 1487. ZOBEL, R.W. : 1107. ZOHM, H. : 339. ZOPPI, F. : 1488. ZOTTER, M. : 369. ZRYD, J.P. : 812.

ORGANISMIC INDEX

Abelmoschus esculentus : 8 16a Abies sp. : 58a, 525, 640 Acacia koa : 10 10 Acer pseud"oplatanus : 191,265,623,670,672,752,812,951,952, 1218, 1429 Acer saccharum : 525 Achyranthes : 1060b Actinidia sp. : 569, 570 Aegilops sp. : 786, 1304 Agropyron elongatum : 685 Agrostis tenuis : 839 Allium sp. : 467, 604, 1047, 1065 Alnus incana : 670 Amaryllis sp. : 1065 Amomum aromaticum : 998 Anagallis arvensis : 167 Ananas sp. : 877, 1388 Anthyllis vulneria : 342 Antirrhinum sp. : 1179 Arabidopsis thaliana : 181,938 Arachis hypogaea : 182,210,211,698, 813a, 998,1255,1256,1257, 1258,1259,1271,

1282, 1321, 1322, 1376, 1377, 1378, 1380, 1381, 1382, 1403, 1404 Argyranthemum : 704 Armoracia (see Cochlearia)

Asparagus officinalis : 444, 445, 449, 499, 1375 Atriplex halimus : 1236 Atropa belladona : 1217, 1219 Avena sp. : 21,22, 25, 234, 373,405,425,470, 523, 536, 756, 785, 832, 833,953,

954, 1080a, 1225, 1226, 1243, 1244, 1413, 1414, 1458, 1469, 1470


Begonia evansiana : 1149 Beta vulgaris : 135, 173,242,325,433,435,441,459,990,991,992, 1079, 1251 Betula alleghaniensis : 473, 582, 586, 587 Boerhaavia diffusa : 998 Brassica japonica : 664 Brassica napus : 330, 555, 624, 626, 627,628,629,641,851,852,853,854,1102,1425,1438 Brassica sp. : 652a, 1064, 1066, 1126, 1223, 1273 Brassicoraphanus : 664 Bryonia dioica : 140, 141, 142, 143, 144 Bryophyllum daigremontianum : 1124

Calamagrostis villosa : 1178a, 1178b Capsicum annuum : 330 Capsicum sp. : 1097 Chamaecyparis lawsoniana : 98 Chenopodium sp. : 71, 374,998, 1236 Chrysanthemum : 704 Cieer arietinum : 1078a, 1448, 1449 Cichorium intybus : 745,746,749,750,927, 1017, 1398 Citrullus sp. : 330, 1408 Citrus sp. : 177, 186, 330,360,365,418,442,690, 716, 1140, 1143, 1252, 1390, 1391

/ Coccini indica : 613a Cochlearia armorica (= Armoracia lapathifolia) : 33, 182, 200, 220, 233, 236, 357, 486,

488, 489, 555, 605, 757, 768, 769, 817, 828, 1006, 1187a, 1423, /424, 1425, 1426, 1427, 1438

Cocos nucifera : 636, 910a CofJea arabica : 480 Coleus blumei : 364, 556, 652 Cordia : 1073a Crotolaria striata : 998 Cucumis mela : 822, 849, 850 Cucumi,\' sativus : 68, 99a, 123,330,356,615,789. 790,874,977, 1052. 1095, 1142.

1192,1303,1451,1452 Cucurbita maxima: 777, 1408 Cucurbita pepo : 251,313,330,352,777. 1024, 1025. \062 Cynara scolymlls : 650 Cyperlls rotllndlls 1060a


Dactyli.r Klomerata : 1053 Datura sp. : 241, 286, 287, 383a, 494, 647, 648, 1124a, 1234, 1238a

Daucus carota . 115, 180, 521, 684, 1284, 1445

Deschampsia ./lexuosa : 1178a, 1178b Diamhus caryophyllus : 190a, 191, 192, 193, 266, 423a, 483, 484, 784

Dionaea muscipula : 1Il 7a Dioscorea composita : 1224

Eleusine corocana : 9518 Euphorbia characias : 834

Fagara coco: 495

FeslUca sp. : 330 Forsythia : 448a Fragaria grandif/ora : 440, 1134

Fraxinus americana : 670 Fraxinus pennsylvanica : 525

Gibasis schiedicana : 1098

Gisekia : 1073b Gladiolus sp. : 1065

Glycine max. : 18, 72, 81, 261, 263, 397,649,733,891,996, 1059, 1068, 1274, 1299, 1329, 1330, 1365

Gossypium hirsutum : 398, 894, 895, 910, 918a, 1232, 1283, 1284, 1399, 1401, 1417, 1442


Helianthus annuus : 238, 330, 638, 639, 1083, 1278, 1280 Helianthus tuberosus : 76,77, 78, 79, 120,427,433,447,521,568,878,879 Hevea brasiliensis : J71, 253, 454, 455 Hibiscus sp. : 330, 998 Hordeum sp. : 21, 24, 25, 30, 53, 54, 58a, 59, 91, 122, 212, 244, 330, 340, 378a,

382, 406, 407, 450, 571, 575, 576, 683, 719, 720, 721, 722, 729, 883, 998, 1055, 1193, 1213, 1294, 1302

Hyacinthus orientalis : 1144 Hydrangea macrophylla : 886

Impatiens balsamina : 137,323,930, 1157 Ipomoea balalas : 108, 110, 115,498,600,601,602,603,844, 1190, 1231, 1314 Ipomoea fistulosa : 213

Lacluca saliva : 913 Lens culinaris (=Vicia lens) : 135a, 136,277,278,279,280,281,282,283,335,336,

337, 372, 411, 412, 413, 428, 432, 438, 439, 441, 443, 450, 451, 577, 674,842,843,871,1015, 1016, 1017, 1028, 1038, 1058, 1307

Lepidium salivum : 477, 478, 1480 Lilium longiflorum : 284 Linum usitatissimum : 384, 385, 386, 387, 388 389, 390, 510, 527, 1353, 1354, 1355,

1356, 1357 Lilchi chinensis : 637 Lupinus sp. : 93, 861, 862, 1050 Lycoper.l'icon esculentum : II, 13, 19, 92, 94, 148, 158, l72a, 216, 274, 330, 331,

356a, 359, 370, 399,458,468, 491, 572, 596, 696, 697, 708, 819, 820, 821, 847, 978, 987, 1010, 1094, 1105, 1106, 1107, 1248, 1249, 1297a, 1326a, 1418


Mangijèra indica : 205, 846, 1383, 1384 MattMola incana : 1133 Medicago sativa : 330, 700, 811 MelUotus alba : 618 Melilotus officinalis : 330 Mercurialis annua : 643, 644, 645, 646, 776 Mnium sp. : 58a Musa sp. : 496, 500, 923

Nicotiana alata : 150, 151, 152, 153, 154, 155, 156, 157 Nicotiana glutinosa : 198 Nicotiana plumbaginifolia : 998 Nicotiana sp. : 1237 Nicotiana tabacum : 5, 9, 29, 75a, 88, 108, 109, 115, 116, 124, 134, 149, 174, 222,

223, 294, 295, 419, 445, 448, 521, 543, 544, 545, 546, 550, 552, 553, 554, 574, 596, 597, 665, 679, 680, 734, 735, 736, 737, 738, 739, 753, 754, 755, 759, 800, 801, 802, 803, 804, 805, 806,807, 808, 870, 921, 942, 948, 976a, 1031, 1036, 1054, 1077, 1078, 1081, 1087, 1088, 1113, 1127, 1129, 1130, 1131, 1161, 1201, 1202, 1203, 1210, 1211, 1212, 1221, 1222, 1239, 1267, 1305, 1327, 1328, 1344, 1393, 1394, 1395, 1406, 1407, 1430, 1478, 1479, 1481

Nicotiana xanthi : 178 Nuphar luteum : 172

Dryza sp. : 206, 207, 212, 358, 462a, 598, 599, 604a, 657, 887, 912. 936. 983. 984. 986,998,999, 1007, 1153, 1184a, 1185, 1253a

i


Panicum mi/iaceum : 330 Papaver somniferum : 14 Parthenocissus tricuspidata : 522 Pelargonium sp. : 436, 521, 1048 Pennisetum typhoideum : 998 Persea americana : 158, 269a, 1333, 1334, 1335, 1385, 1386, 1387, 1389, 1392 Petunia sp. : 934, 935 Phalaenopsis amabilis : 1343 Phalaris arundinacea : 1370, 1371 Pharbilis ni! : 955, 1277, 1281, 1473, 1474 Phaseolus aureus : 8,62, 196, 197,312,404,728, 1103, 1143, 1204, 1341 Phaseolus mungo : 214,215,493,933 Phaseolus radiatus : 61, 1070, 10711 Phaseolus vulgaris : 36, 37, 38, 39, 40, 75, 146, 168, 260, 262, 285, 292, 330, 359,

501, 503, 514, 515, 581, 597, 775, 845, 858, 859, 880, 889, 890, 911, 956, 1045, 1076, 1220, 1342, 1348, 1400, 1420

Picea abies : 369, 482, 525, 672 Picea excelsa : 53 Picea glauca : 383, 525, 1349 Picea sp. : 923 Pinus banksiana : 1073 Pinus elliottü : 1435, 1436a Pinus nigra : 53, 58a, 670 Pinus palustris : 1245 Pinus radiala : 446 Pisum salivum : 21, 53, 54, 54a, 55, 56, 57, 58a, 59, 82, 113, [39, 147, 169, 188,

237, 258, 267, 268, 274, 275, 276, 297, 306, 307, 330, 373, 391, 392, 424, 441, 463, 547, 548, 549, 551, 588, 606, 6[6, 697a, 722, 796, 797, 841, 863, 919, 962, 963, 964, 979, 981, 1078a, 1082, 1108, 1109, 1110, 1139,1143,1146, J 148, 1154, 1155, 1247, 1301, 1346, 1347, 1372, 1397, 1482

Pinus sp. : 640, 670, 677, 774, 946, 1178a Pinus strobus : 525, 670 Pinus ~ylveslris : 43, 670, 946 Pinus laeda : 1245 Poinseuia : 1428 Populus deltoides : 469, 525 Populus niKra : 101,931,932 Populus sp. : 191,677,774, 1453 Populus lremuloides : 510, 525, 1165, 1447

1ORGANISMIC INDEX 309

Prunus avium : 1046 Prunus persica : 396, 1043a Prunus sp. : 444, 445, 1063, 1166, 1444

Pseudotsuga sp. : 640, 672

Pseudotsuga menziesii : 245, 632, 670 Pyrus communis : 158, 399, 400, 402, 1317

Pyrus malus: 125,353,471,525, 729b, 758, 947, 1135, 1320

Pyrus sp. : 1074

Quercus sp.: 670, 848

Raphanus sativus : 221, 592, 664, 902, 903, 904, 967, 998

Ricinus communis : 330, 1471, 1477

Robinia pseudoacacia : 591 Rosa: 712, 713

Rumex acetosa : 839

Saccharum o.fficinarum : 99 Salix sp. : 510, 5 15a Salix tetrasperma : 100

Salvia splendens : 1133 Secale cereale: 330, 405, 578, 1075, 1298

Sedum album: 187a Sifene alba : 747, 748

Sifene cucubalus : 839 Sifybum marianum : 475

Sinapis alba : 52, 573, 1174, 1174a, 1176


Solalllllll IIIl.'lolIgl.'na : 330. 651 SolallulIl /uhl.'rosulIl : 127, 129, 130, 161, 218, 296,410,423,465,985, 1137, 1272,

1284, 1326, 1340, 1439, 1484, 1485 Sonlll.'ra/ia alha : 614 SOI·hlls aucuparia : 525 Sorghlllll sp. : 330, 761, 765, 998, 1138, J164, 1262, 1263 Sparlina al/ernf/lora : 461 a Spartina paœns : 461 a Spinacia sp. : 41, 305, 339, 414, 415, 444, 445, 479, 658, 659, 660, 661, 982, 1017,

1018, 1019, 1020, 1021, 1022, 1023, 1026, 1189 Syringa l'ulgaris : 525

Tabernaemomana coronaria : 998 Tagetes pa/ula : 1415 Taraxacum officinale : 675 Taxus cuspidata : 525 Thea sinensis : 1309, 1331 Theobroma cacao : 655 Thlaspi alpestre : 839 Tradescantia sp. : 1041, 1065 Trigonella foenum graecum : 60, 63, 64, 65, 66, 856, 857 Triticale sp. : 259, 760, 1075 Triticum aeslÎvum : 14, 15,21,23,95, 133, 146a, 189, 191, 199,201,203,264,270,

271, 271a, 330, 371, 394, 405, 409, 452, 506, 526, 578, 630, 631, 662, 683, 685, 686, 687, 699, 705, 706, 787, 788, 792, 835, 882, 998, 1043, 1180,1181,1227,1228,1229,1230,1241,1315,1316,1434,1487

Trilicum durum : 619,687, 1075 Tulipa sp.: 1145

Vlmus mOn/ana : 670


Vaccinium corymbosum : 399 Vaccinium myrtil/us : 1178a, 1178b

Vaccinium vitis-idaea : 1178a, 1178b Vicia faba : 502, 610, 1078a, 1141

Vicia sativa : 330 Vicia vil/osa : 330 Vigna mungo : 1115

Vigna sinensis : 773 Vigna sp. : 1279 Vitis sp. : 71, 691, 692

Xanthium pennsylvanicum : 209

Xanthium strumarium : 793

Zea mays : 10,17,53, 58a, 90, III, 114, 160a, 165,237,254,311,321,330.373, 395, 405, 425a, 425b, 434, 441, 485, 541, 613, 676, 682, 689, 742, 811,

830,831,914,949,980,993,994,998,1010,1056,1139, 1194, 1195, 1196, 1197, 1198, 1254, 1374, 1405, 1483

SUBJECT INDEX

Abscisic acid (elTect ot): 411, 412, 413, 439,716,855,1316.

Abscission : 2, 255, 442, 514a, 515, 543, 544, 545, 546, 550, 553, 554, 1045, 1046, 1097, 1384, 1420, 1444.

Acetylcholine: 1015, 1019, 1195.

Aging : 35, 112, 146, 149, 158, 167, 221, 457a, 471, 614, 642, 657, 659, 729a, 998, 1100, 1136, 1137, 1231, 1274, 1343, 1348, 1390, 1407.

Aigae : 7, 166,466, 563a, 864, 865, 915, 916, 917, 918, 1009, 1029, 1207, 1214.

Amino acid composition and sequence 680, 851, 853, 854, 902, 1423, 1424, 1425, 1426, 1427.

Anaerobiosis : 219, 328.

Anti-peroxidase : 132, 164, 187,236,490,837,972, 1006, 1167, 1235, 1270.

Apical dominance : 18.

Apo-peroxidase : 233, 327, 654, 680, 702, 709, 802, 853, 854, 902, 1034, 1093, 1293, 1362, 1423, 1424, 1424a, 1425, 1427.

Ascorbate peroxidase : 54a, 54b, 54c, 673, 1207.

Assay: 229, 239, 358, 377, 391, 421, 487, 558, 779, 838, 888, 943, 988, 1000, 1392.

Auxin (effect ot) : 42,66, 108, 115,222,267,268,278,281,309,337,360,372,428, 442, 450, 551, 588, 675, 689, 737, 748, 753, 754, 756, 812, 821, 871, 934,963,1071,1113,1155, 1219, 1405, 1406, 1429, 1434.

Auxin protectors : 213,427,436,456,480,497,684,744,934,955, 1041, 1142, 1233, 1277, 1278, 1279, 1280, 1281, 1305.

1


Bacteria : 530, 1029a, 1037, 1324.

Bactericidal function : 48, 380, 634, 635, 865, 1001, 1122a, 1319, 1323, 1324, 1364, 1366, 1373.

Biosynthesis : 171, 267, 268, 532, 674, 757, 783a, 805, 824, 956, 1108, 1190, 1198, 1271, 1315, 1376, 1378, 1380, 1381, 1382, 1404, 1458.

- inhibitors : 76, 78, 114, 323, 581,954, 1108, 1190, 1198, 1381, 1382.

Bromoperoxidases 7, 50, 563a, 1009.

Browning: 637, 688, 1166.

Bryophytes : 460, 565, 612, 1044, 1170, 1246, 1250, 1352

Bud formation: 448, 569, 745, 750, 800, 806, 927, 938, 1327, 1328, 1398.

Calcium: 52a, 56, 133,352,454,530,619,966, 1016, 1024, 1061, 1424a.

Cal1us : 75, 75a, 181, 242, 448, 676, 690, 734, 735, 736, 737, 738, 739, 800, 806, 807,938,942,951, 1087, 1161, 1327, 1328, 1406, 1447.

Cancer: 240,316, 317,341,666, 1027.

Cel1 cultures: 36, 37, 38, 39,40, 74, 265, 414, 415, 623,676, 679, 680, 698, 747, 748,809,812, 813a, 880, 951, 952, 1036, 1054, 1112, 1113, 1210, 1211, 1212, 1217, 1218, 1219, 1255, 1256, 1257, 1376, 1377, 1378, 1380, 1381, 1382, 1403, 1404, 1429, 1483.

Cereal seeds : 212, 340,371,405, 598 599, 706, 707, 719, 720, 721, 729, 760, 761, 936,986, 1067, 1075, 1185, 1187, 1230, 1294, 1316.

Characterization : 7,4/, 247, 276, 319, 334, 345, 370, 385, 463, 528, 598, 605, 609, 610, 619, 650, 679, 68/, 682, 696, 828, 851, 873, 880, 901, 903, 904, 915, 923, 942, 980, 1006, 1080, 1103, 1128, 1138, 1146, 1209, 1211, 1240, 1259, 1352, 1369, 1459 1463.

Chemical studies : 6, 228, 308, 344, 361, 379, 461 a, 492, 533, 606a, 606b, 628, 731, 732, 813, 814, 815, 816, 872, 920, 925, 950, 968, 969, 1104, 1156, 1173, 1205, 1311, 1454, 1455, 1460, 1460a, 1462, 1474a.

SUBJECT INDEX 315

Chemical treatments : 52a, 54c, 122, 135, 136, 180, 181,215,3[0,324,549,775,877, 912,953, 1129, 1192, 1219, 1302.

Chemiluminescence : 34,45,291,511, 1057.

Chloroperoxidase : 246, 505, 1325.

Chloroplasts : 609,613,919, 1128.

Cold tolerance : 641, 700, 1194.

Coleoptile : 425, 470, 1431.

Compound J : 31a, 32, 106, 225a, 249, 289, 346, 347, 531, 534, 535, 563, 625, 626, 629,633,681,813,897,920,960,1004,1069,1120,1121, 1150, 1268, 1275, 1276.

Compound JI : 249, 256, 257, 331a, 347, 531, 534, 535, 897, 920, 920a, 960, 1121, 1122, 1276.

Compound JII : 33la, 429, 1033, 1312.

Crown-gall and other tumors : 9, 137, 260, 287, 524, 956, 1060, 1073a, 1073b, 1083, 1124a, 1125.

Cyanide : 250,347, 815.

Cytochemical.techniques : 10, 28, 31, 159, 179, 224, 225, 367, 376, 393, 487, 559, 561, 567, 711, 764, 779, 791, 866, 867, 884, 949, 958, 970, 989, 1014, 1090, 1118, [183, 1184, 1216, 1282, 1285, 1286, 1287, 1289, 1290, 1292, 1337, 1368, 1421.

Cytochrome c : 434,885,944, 1151, 1441.

Cytochrome c peroxidase : 170,252,328,362,363, 783a, 885, 941, 945. 1437.

Cytochrome P-450 : 354, 589, 590, 705, 961, 1091, 1092.

Cytokinins (effect of) : 38, 39, 40, 61, 66, 99a, 197, 278, 281, 337, 412, 439, 450, 521,588,734,737,739,749, 1129, 1170, 1193, 1316.


2,4-D (effect of) : 38, 39, 40, 60, 180, 181,394,722,736,748,1005, 1113, 1253, 1429.

Development : 146,209,356,396,463,468,469, 572, 643, 720,847, 848,998, 1075, 1158,1220,1414.

Differentiation : 51, 52, 127, 128, 161,311,445,448, 462a, 503, 528, 569,612,644, 658, 800, 806, 878, 879, 927, 938, 1149, 1158, 1327, 1328, 1336, 1403, 1416, 1447, 1484.

Dormancy : 447, 452, 506, 691, 758, 936, 1047, 1317, 1320.

Dwarfism : 874, 1227.

Electrophoresis : 21, 130, 175,358,597,623,664,767,768,803,818,881,883,931, 1017, 1200, 1234, 1291, 1393.

Embryos : 443, 599, 758,947,959, 1135, 1317, 1320, 1445.

Endoplasmic reticu1um : 188, 191,265,320,467,515,544,952,959, 1024, 1381, 1420, 1480.

Ethylene (effect of) : 1,2, 5, 108, 110, 115, 188,218, 271a, 337, 364,442,498,499, 544, 545, 548, 550, 551, 552, 553, 554, 588, 600, 692, 716, 857, 894, 981,1030,1095,1109,1110,1155,1192.

- synthesis : 172a, 398, 571, 653, 697a, 708, 728, 762a, 763, 773, 788, 819, 820, 821, 1418, 1464.

Extraction: 294, 440,510,586,712, 723a, 738, 796, 813a, 937,1017,1171,1309, 1380, 1388, 1391.

Fern: 762.

Flowering : 444, 445, 448, 479, 658, 659, 1018, 1019, 1020, 1022, 1184a, 1328.

Fruit development and ripening : 125, 158, 396, 399, 400, 402, 471, 496, 500, 637, 705,708,720,721,846,847,923, 1068, 1075, 1383, 1384.

SUBJECT INDEX 317

Gene expression: 11,95, 157, l60a, 271, 271a, 420,578,685,686,786,984, 1007, 1107, 1164, 1180, 1237, l238a, 1315, 1470.

Genetics 13, 22, 23, 24, 25, 53, 58, 154, 165, 177, 211, 241,245, 254, 356a, 365, 378a, 382, 383, 383a, 384, 385, 386, 387, 388, 459, 460, 461, 494, 574, 652a, 761, 793, 797, 830 832, 874, 914, 934, 935, 939, 948, 983, 984, 1055, 1107, 1201, 1203,1223, 1226, 1237, 1238, 1245, 1254, 1304, 1333, 1334, 1335, 1354, 1355, 1356, 1357, 1428, 1469, 1470.

Geographical distribution: 254, 523,1105,1107, 1178a, 1178b,1213, 1225, 1349.

Gennination : 9, 30,43, 212, 312, 443, 452, 506, 649, 706, 986, 999, 1073, 1080a, 1185, 1187, 1204, 1227, 1228, 1229, 1247, 1294, 1320, 1322, 1342, 1477.

Gibberellins (efTect of) : 113,188,310,415,551,716,735,737,962,963,964,1022, 1071, 1133, 1157, 1316.

Glutathione peroxidase : 474, 516, 783.

Glycoprotein : 162,233,276,757, 1089, 1187a, 1376, 1424, 1425.

Golgi apparatus: 20, 1JO, 161, 191,265,467,515,1480.

Gradient in plants: 144,201,296,390,485,502,638,658, 1141, 1328.

Gravity (efTect of) : 504,524, 1415.

Growth 82, 149, 199, 202, 203, 208, 311, 321, 372, 373, 394, 424, 432, 433, 439, 450, 451, 502, 549, 615, 652, 761, 855, 947, 1015, 1071, 1072, 1088, 1142, 1154, 1155, 1192, 1405, 1406, 1416, 1447, 1453, 1483.

Growth retardants (efTect of) : 133,428,451,964, 1050, 1133,1141.

Halides 12, 85, 117, 118, 204, 246, 541, 593, 611, 627, 668, 715, 759, 906, 907, 908,909, 1035, 1040, 1062, 1084, 1120, 1122, 1268, 1323, 1324, 1412.

Herbicides: 122, 123, 1303, 1307.

Honnonal interaction: 18,66, 126a, 168,312,364,439,443,450,665,716,737,947, 1075a.

Honnones (animais) : 3, 26, 27, 67, 103, 175,227,240,316,341,621,622,666,667, 668, 780, 781, 782, 868, 1295, 1446.

Hybrids : 146a, 378a, 388, 830, 914, 1081, 1356, 1453, 1473.

318 PEROX1DASES 1970/1980

Hydrogen peroxide metabolism 158, 1220.

- formation: 138,357,488, 488a, 489, 517, 518,694,808, 1103, 1308.

Hydroxylation : 271b, 519a, 581, 606, 765,997, 1008, 1009, 1242.

Hydroxyproline : 283, 769, 850, 981, 1109, 1110, 1434.

IAA catabolism : 58a, 126a, 137, 168, 214, 237, 238, 244, 255, 274, 275, 336, 353, 356, 364, 373, 398, 399, 400, 406, 407, 411, 432, 436, 438, 458, 583, 587, 602, 612, 616, 632, 697, 742, 743, 773, 775, 789, 790, 812, 855, 856, 857, 861, 862, 895, 977, 987, 1018, 1041, 1050, 1056, 1064, 1141, 1149, 1169, 1231, 1372, 1398, 1429, 1439.

IAA oxidase isoforms : 169, 258, 269a, 470, 473, 584, 585, 677,734, 735, 736, 774, 818,931,962,1018,1038, 1080a, 1141, 1210, 1211, 1255, 1256, 1257,1474.

- localization : 91, 94, 134.

IAA oxidation : 90, 200,429, 430, 431, 437, 440, 456, 497, 522, 582, 601, 603, 697, 740, 741, 744, 752, 785, 787, 841, 842, 843, 852, 869, 875, 924, 933, 1066,1101,1134,1142,1148,1300,1371,1410,1461.

Immobilized peroxidases : 69, 73, 96, 1163.

Immunochemical studies : 46, 56, 57, 58, 182,286,287,645, 1124a, 1285, 1286, 1377.

Infection (reaction to) : 72, 81, Ill, 114, 173, 189, 205, 206,238, 260, 261, 266, 269a, 322, 335, 336, 407, 408, 409, 410, 423a, 425a, 425b, 454, 455, 458, 465, 482, 483, 484, 491, 498, 571, 595, 611, 617, 630, 631, 636, 655, 683, 792, 822, 835, 844, 849, 850, 858, 859, 889, 890, 918a, 967, 1058, 1060a, J060b, 1082, 1097, 1126, 1127, 1153, 1165, 1180,1181, 1186, 1189,1224, 1253a, 1264, 1265, 1340, 1363, 1363a, 1364, 1366, 1366a, 1383, 1385, 1386, 1387, 1389, 1390, 1399, 1417, 1430, 1458.

Inflammation (animais) : 333, 710.

Inheritance : 756, 831, 1244, 1245, 1469.

Inhibitors 137, 197a, 288, 342, 464,476, 477, 478, 601, 619, 684, 744, 749, 826, 827, 1029, 1285, 1287, 1356, 1386, 1396.

Iodide peroxidase 85, 915, 922.

Ion deficiency 306.

SUBJECT INDEX 319

Ionie treatments (effect of) : 54, 54a, 54b, 55, 58a, 59, 141, 143, 186,244,308, 729b, 733,1013,1115,1468.

Irritation: 140, 141, 142, 143, 144, 148.

Isoelectric focusing : 258, 261, 298, 299, 300, 30 l, 302, 303, 584, 585, 803, 980, 1039, 1130, 1131, 1132.

Isoperoxidase patterns: 52, 53, 75, 75a, 116,125,172,311,313,338,365,381,389, 425, 470, 475, 494, 500, 502, 632, 640, 677, 774, 845, 903, 1054, 1098, 1298, 1331, 1355, 1474,

[soperoxidases in related species or cultivars : 14, 15, 22, 23, 24, 25, 182, 210, 211, 234, 241, 254, 259, 383a, 384, 494, 604a, 687, 704, 712, 713, 777, 833, 935, 1055, 1081, 1106, 1191, 1223, 1226, 1239, 1243, 1304, 1428.

Kinetics : 16, 33, 65, 70, 217, 257a, 289, 329, 343, 370, 531, 594, 629, 730, 752, 807, 933, 1033, 1056, 1066, 1085, 1088, 1121, 1122, 1150, 1359.

Lactoperoxidase : 197a, 907, 1003, 1062.

Leaf : 172, 174, 209, 221, 294, 321, 348, 369, 469, 650, 651, 658, 722, 948, 990, 991,998, 1031, 1236, 1298, 1331, 1398.

Light (effect of) : 54a, 92, 93, 122,292,613,745,746,749,755,784,799, 1137. 1193. 1229, 1237.

Lignification : 20, 139, 190a, 192, 487a, 499, 503, 507. 518, 525, 529, 564. 828a. 878. 879, 890a, 926, 967, 1074, 1099, 1214. 1261, 1370, 1371, 1436. 1436a.

Localization (animal cells) : 4, 28, 121, 184, 185, 248. 269, 293, 316, 366. 375. 417. 467, 468, 539, 557, 560, 662, 663. 714. 798. 823. 825. 836. 890. 957. 1042, 1114, 1116, 1296. 1297, 1351, 1419. 1452.

Localization (plant cells) : 94. 124a. 147. 155. 190. 190a. 191, 192. 193. 253. 264. 265, 266, 391, 392. 465. 513. 514. 515. 543. 544. 556. 645. 739. 762. 834, 858. 859. 863, 910. 919. 949, 951, 952. 979. 990. 991, 992. 1046. 1052. 1053, 1065,1246, 1262. 1399, 1402. 1408. 1420, 1442. 1480.

320 i·


Mechanisms of reaction : 90, 105, 106, 107, 195,231, 232, 249,250, 256, 257, 315, 347a, 422, 437, 453, 481,519,594,678,697,924,928, 1002, 1035, 1051, 1096, 1101, 1151, 1152, 1162, 1312, 1338, 1411, 1461.

Membrane-bound : 143,282,496,538,739, 847,951,952,991,992,993,994, 1016, 1023, 1024, 1372, 1381.

Mitochondria : 279, 434, 474, 864.

Molecular interactions: 6, 327, 625, 627, 702, 1002, 1162, 1172, 1456.

Morphactin (effect of) : 63, 930, 1072, 1482.

Mutants: 19,207,847, 910a, 987, 1145, 1179, 1248, 1249, 1297a.

Myeloperoxidase : 893, 965, 995a, 1122a, 1123, 1308.

Mycetes : 332,335,336,724,770.771,941, 1058, 1182, 1332, 1416.

Nitrate reductase activity : 31 a, 607, 608, 10 II, 1012, 1115, 1254.

Nuclear magnetic resonance : 724a, 727, 751, 897, 898, 899.

Nucleic acids : 87, 88, 621, 740, 753, 860, 956, 1409.

Nutrition: 98, 244, 307, 638, 733, 887, 895, 1115, 1140, 1273.

Oscillatory reactions : 291, 974, 975, 975a.

Ozone (effect of) : 262. 263, 285, 359, 1329, 1330.

SUBJECT INDEX 321

Peroxidase-like : 378,418,540, 701, 1049, 1440.

Pheno1ics : 74, 84, 297, 321, 389, 414,512, 519a, 547, 573,603,638,723,744,746, 787,795,856,876.996, 1060, 1099, 1100, 1134, 1142, 1148, 1161, 1177, 1178,1189,1202,1233,1258,1260,1261,1278,1281, 1314, 1366, 1418, 1435, 1440, 1476.

Photoperiod : 167,295, 462a, 1018, 1022, 1149, 1184a, 1413, 1453.

Phototropism : 504.

Physico-chemical studies : 225a, 492, 555, 563, 624, 654, 724a,751 , 810, 897, 898, 899,900,1147,1162, 1199, 1206, 1293, 1310, 1438, 1474a.

Phytochrome: 592,660,661,1019,1020,1023,1025,1174, 1174a, 1175, 1176, J 194, 1195,1196,1197,1198,1237.

Plant parts: 75, 75a, 135a, 494, 495, 502, 1139, 1344, 1442.

Plant selection: 165, 177, 1010, 1333.

Ploidy : Il, 338, 882, 896, 1043, 1238a, 1251, 1304.

Pollen tube: 149, 150, 151, 152, 153, 154, 156,284,324.

Pollution: 187a, 359, 395, 482, 509, 579, 580, 670, 671, 672, 733, 759, 811, 839, 911, 913, 946, 1048, 1178a, 1232, 1330, 1427a.

Proteins (etfect on) : 44, 183,309,457, 1062, 1436.

Protoplasts : 804.

Purification: 7, 17,41,47, 162, 230, 233, 272, 317, 319,326,619,650,696,794, 915,976, 1006, 1089, 1132, 1138, 1160, 1207, 1250, 1309, 1326a.


Radiations uv : l72a. 501, 548. 553.

- x : 222.

- y : 1326, 1416.

Rapid effects : 660, 661, 1019. 1020, 1021, 1022, 1023, 1025, 1026.

Reactions catalyzed by peroxidases : 83, 84, 85, 86,97, 163,217,226,239, 271b, 273, 325, 349, 35~ 368, 421~ 422, 423, 457~ 462, 463, 481, 520, 566, 573, 605, 6[8, 647, 648, 656, 681a, 682, 703, 723, 730, 766a, 795, 828, 840, 872, 940, 971, 973, 1036, 1069, 1076, 1085, 1086, 1087, 1088, 1119, Il 43a, 1177, 1178, 1188, 1202, 1215, 1339, 1440, 1443, 1448, 1449, 1457, 1467, 1472, 1486.

Resistance against infection: 13, 17,81,93,270,271, 271a, 355, 374, 575, 576, 889, 921,982, 1079, 1094, 1180, 1181, 1221, 1222, 1340, 1365. 1370, 1371, 1394, 1401, 1439.

Respiration: 500, 598, 599, 733, 999, 1390, 1406.

Ribosomes: 191,279, 428, 467, 952, 1028, 1066, 1480.

Root : 124a, 177,219,251,277,280,338,348,391,392,432,435,441, 502, 591, 615,616, 675, 742, 861, 862, 1141, 1187a, 1241, 1301, 1374.

- nodules: 861, 862, 863, 979, 1046, 1047, 1059, 1060, 1346.

Rooting : 100, 101, 120, 168, 196, 197,214,215,323,404,444,445,446,448,449, 493,568,652,886,930,931,932, 1041, 1063, 1217, 1328, 1375.

Secretion: 2, 135a, 227, 415,426,467,537,539,557,562,891, 976a, 1061, 1117a, 1382, 1480.

Seeds : 21, 330, 508, 640, 1043, 1078a, 1143.

Separation of isofonns : 162,233,381,384,397,679.

Sex expression: 613a, 643, 645, 646, 658, 659, 776, 790, 1018,1095, 1192.

Substrate specificity : 220, 605, 682, 1002, 1036, 1214, 1393, 1476.

Sulphydryl : 44, 61, 62, 64, 1070, 1071.

SUBJECT INDEX 323

Temperature (effect 01) : 135, 295, 306, 515a, 639, 641, 699, 700, 784, 977, 1124, 1182, 1227, 1317, 1321, .

Thermal stabi1ity : 29,96,223,303,304,305,339,778,802,995, 1056, 1313, 1321, 1358, 1361, 1369, 1397, 1479.

Thigmomorphogenesis 140, 141, 142, 143, 144.

Tissue culture: 51,75, 75a, 87, 180, 181,242,360,448,449,503,569,570,676,690, 729b, 734, 735, 736, 737, 745, 750, 755, 784, 800, 806, 905, 927, 938, 985, 1043a, 1054, 1129, 1130, 1131, 1159, 1252, 1327, 1328, 1360, 1406, 1407, 1416, 1445, 1447, 1481, 1483.

Tuberization : 338, 433, 435, 447.

Uptake in animal tissues: 243, 314, 526, 695, 717, 726, 1117, 1266.

Vacuoles: 124, 191,251,265,467,486,514,951,993,994, 1052, 1053, 1480.

Virus: 29,68, 71, 80, 81, 89,99, 109, 178, 198,420,773, 1221, 1222, 1267, 1299, 1341, 1366a, 1394, 1395, 1400, 1430, 1450, 1451.

Wall: 72, 109, 115, 144, 161, 192, 193,223,261,264,284,357,391,414,415, 423a. 467,485, 488a, 489,514,521,550,604,725,769,801.804.805. 828a, 849,850,870,951,952,993, 1044, 1053, 1078, 1109, 1110, 1271, 1283, 1284, 1434, 1435, 1436, 1436a, 1478, 1479, 1480.

Water potential : 274.

Water stress: 212, 275, 978.

Wound : 76, 77, 78, 79, 108, 109, 110, Ill, 113, 114, 115, 116,127, 129, 322. 498, 588,753,754,766,844,978, 1099, 1144, 1314, 1326.

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peroxidases ( peroksida )