512 PATENT ABSTRACTS

5114768 5114857

S U R F A C E S W I T H R E D U C E D P R O T E I N I N T E R A C T I O N S

Sally Swedberg assigned to Hewlett-Packard Company

A solid surface that is exposed to protein solutes in use, such as medical implants or capillary tubes useful in capillary zone electrophoresis, is defined by or carries a polymer. An interracial layer is covalently bound to the polymer and functions to reduce interactions between the sur- face and protein solutes. The interfacial layer in- cludes either a hydratable amphoteric phase or a plurality of halogen atoms bound in the interfa- eial layer through at least one heteroatom.

A C T I N O M A D U R A H I B I S C A M I C R O O R G A N I S M U S E F U L F O R P R E P A R I N G S E R I N E A N A L O G S

O F BU-3608 A N T I B I O T I C S

Yosuke Sawada, Masatoshi Kakushima, Maki Nishio, Takeo Miyaki, Toshikazu Oki, Tokyo, Japan assigned to Bristol-Myers Company

Disclosed are antibiotics BU-3608 FA-1 and FA-2 and alkyl derivatives thereof. These com- pounds are useful as antifungal agents. BU-3608 FA-1 and FA-2 are produced from Ac- tinomadura hibisca in a medium containing a source of D-serine.

5114842

P E P T I D E S A N D A N T I B O D I E S T H A T I N H I B I T P L A T E L E T

A D H E S I O N

Edward F Plow, Mark H Ginsberg assigned to The Scripps Research Institute

A polypeptide analog capable of immuno- logically mimicking a linear hGPIIb antigenic determinant expressed when platelet-associated GPIIb-IIIa binds fibrinogen is disclosed. An antibody that immunoreacts with the poly- peptide and hGPllb when hGPIIb is present as a platelet-associated GPPIb-llla/fibrinogen com- plex is also disclosed. Further disclosed are dia- gnostic systems and methods for assaying fibrinogen-bound platelets in a vascular fluid sample using the potypeptides and/or antibodies of the invention.

5114845

A S S A Y S F O R P L A S M I N O G E N A C T I V A T O R I N H I B I T O R A N D

S O L U B L E F I B R I N

Mats G Ranby, Umea, Sweden assigned to Bio- pool International Inc

The present invention relates to an improved method for measuring soluble fibrin utilizing a genetically modified tissue ptasminogen ac- tivator protein as a substrate.

5114863

I M M U N O S O R B A N T A S S A Y F O R A L P H A - 1 - A N T I T R Y P S I N , K I T

E M P L O Y I N G S A I D A S S A Y , M O N O C L O N A L A N T I B O D Y T O

A L P H A - 1 - A N T I T R Y P S I N , A N D H Y B R I D O M A F O R P R O D U C I N G

S A I D M O N O C L O N A L A N T I B O D Y

Candace C McCombs, Joseph P Michalski, Wil- liam R Gallaher, James Thompson assigned to Board of Supervisors of Louisiana State Univer- sity & Agricultural & Mechanical College

A double antibody sandwich immunosorbent assay for detecting alpha-l-antitrypsin ( al- phalAT) comprising the steps of: (1) reacting (a) a first-species-of-animal antibody to alphalAT with (b) a solid substrate; (2) reacting (a) al- phalAT in a sample suspected of containing alphalAT with (b) the first-species-of animal polyclonal antibody to alphalAT; (3) reacting (a) a second-species-of-animal antibody to al- phalAT with (b) the alphalAT in a sample suspected of containing alphalAT; (4) reacting (a) a labelled antibody comprising a first-species- of-animal antibody to an antibody from a second species of animal with (b) the second- species-of-animal antibody to alpha l AT; and (5) detecting the amount of labelled first-species-of- animal antibody to antibody from the second species of animal that reacted with the second- species-of-animal polyclonal antibody to al- pha 1 AT; provided that the first species of animal and the second species of animal are not the same in a given assay; and provided that steps (1) to (4) can be conducted in any order so as to result in a complex comprising: (i) the substrate complexed

PATENT ABSTRACTS 513

to (ii) the first-species-of-animal antibody to al- phalAT complexed to (iii) the aiphalAT com- ple×ed to (iv) the second-species-of-animal antibody to alphalAT complexed to (v) the labelled antibody. The antibodies used in the as- say can be polyclonal antibodies or monoclonal antibodies. A kit for detecting alphalAT com- prising reagents for conducting the above described assays. A monoclonal antibody having specific reactivity to alphalAT, the antibody being further characterized in that it exhibits substantially no cross reactivity with albumin. A hybridoma that produces the above described monoclonal antibody.

5114923

RECOMBINANT TECHNIQUES FOR PRODUCTION OF NOVEL

NATRIURETIC AND VASODILATOR PEPTIDES

Jeffrey Seilhamer, John A Lewicki, Robert M Scarborough, J Gordon Porter assigned to California Biotechnotogy Inc

5114920

BU-3292T A N T I B I O T I C S

Kok Sugawara, Yuji Nishiyama, Koji Tomita, Masataka Konishi, Toshikazu Oki, Saitama, Japan assigned to Bristol-Myers Squibb Co

New antibiotics designated BU-3292T A and B are provided which exhibit antimicrobial activity and also inhibit the growth of tumors in experi- mental animal systems. BU-3292T A is produced by fermentation of Elytrosporangium sp. nov. (ATCC 53784) while the BU-3292T B com- pound is obtained by oxidation of BU-3292T A.

5114922

P O L Y P E P T I D E S W I T H A N ANTICOAGULANT A C T I V I T Y

Reinhard Maschler, Verena Steiner, Markus G Grutter, Fritz Raschdorf, Oldenburg, Federal Republic Of Germany assigned to Ciba-Geigy Corporation; UCP Gen-Pharma

Novel polypeptides, designated hirullins, have a strong antithrombic activity and can therefore be used for the therapy and prophylaxis of thromboses. Said compounds are isolated from the leech Hirudinaria manillensis or are pro- duced by conventional peptide synthesis or by recombinant DNA techniques.

PCT No. PCT/US89/02373 Sec. 371 Date Feb. 2, 1990 Sec. 102(e) Date Feb. 2, 1990 PCT Filed May 31, 1989.The cDNA sequence encoding porcine brain natriuretic peptide and related genes encoding canine and human peptides with natriuretic activity are disclosed. The gene is shown to make accessible the DNAs encoding analogous natriuretic peptides in other ver- tebrate species. The genes encoding these NPs can be used to effect modifications of the sequence to produce alternate forms of the NPs and to provide practical amounts of these pro- teins. The NPs of the invention can also be syn- thesized chemically. The invention peptides have the formula: See Patent for Chemical Structure (1) Ite- Gly/ -Ser- Leu/ -Ser-Gly-Leu-Gly-Cys- R2SerSer wherein RI is selected from the group consisting of: See Patent for Chemical Structure His/ - Lys/ -Ser-Gly-;Arg/Asp/GtnGly Met/ - His/- Lys/-Ser-Gly-;Arg/Asp/ValGlnGly Thr/- Met/ His/ Lys/ -Ser-Gly- ;Arg/Asp/MetValGlnGly Lys- Thr/- Met/- His/ - Lys/ -Ser-Gly-;Arg/Asp/MetValGlnGly Pro- Lys- Thr/ - Met/ - His/ - Lys/ -Ser-Gly- ;Arg/Asp/MetValGlnGly Ser-Pro-Lys- Thr/ - Met/ His/ Lys/ -Ser-Gly- ;MetValGlnGlyArg/Asp/or a 10- to 109-amino acid sequence shown as the native upstream sequence for porcine, canine or human NP in FIG. 6, or a composite thereof; R2 is (OH), NH2, or NR'R" wherein R' and R" are indepen- dently lower alkyl (I-4C) or is See Patent for Chemical Structure Asn/ -ValLys Asn/ -Val- LeuLys Asn/ -Val-Leu-ArgLys Asn/ -Val-Leu- Arg- Arg/LysLys Asn/ -Val-Leu-Arg- Arg/ - Tyr/LysLysHis or the amides (NH2 or NR'R") thereof, with the proviso that if formula (1) is See Patent for Tabular Presentation PS and RI is Asp-Ser-G/y-, R2 cannot be Asn-Val-Leu-Arg- Arg-Tyr. The peptides of the invention can be formulated into pharmaceutical compositions and used to treat conditions associated with high extracellular fluid levels, especially congestive heart failure.