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Chemistry LaboratoryChemistry Laboratory
It is often necessary to measure several blood chemicals to establish a pattern of abnormalities.
A wide range of tests can be grouped under the headings of enzymes, electrolytes, blood sugars, lipids, hormones, proteins, vitamins, minerals, and drug investigation.
General Biochemical General Biochemical ProfilesProfilesProfiles are a group of select
tests that screen for certain conditions◦Chemistry panels◦Cardiac markers (MI) ◦Electrolyte panel
Kidney functions, disease◦BUN, Phosphorus, LDH, Creatinine,
creatinine clearance, total protein, A/G ratio, albumin, calcium, glucose, CO2
Lipids (coronary risk)◦Cholesterol, triglycerides, HDL,
lipoprotein electrophoresis (LDL, VLDL, HDL)
Liver function, disease◦Total bilirubin, alkaline
phosphatase, GGT, total protein, A/G ratio, albumin, AST, LDH, viral hepatitis panel, PT
Thyroid function◦T3 uptake, free T4, total T4, T7, FTI,
TSHBasic metabolic screen◦Chloride, sodium, potassium,
carbon dioxide, glucose, BUN, creatinine
Syndrome X (metabolic syndrome)◦Blood lipid; glucose; cholesterol ◦Definition of metabolic syndrome
includes three or more of the following:
abdominal obesity (>40 inches in men and >35 inches in women);
HDL cholesterol (<40 mg/dL in men or <50 mg/dL in women);
blood pressure >130/85 mmHg; fasting glucose > 110 mg/dL
Acute Hepatitis Panel (ACUTE HEP)Hepatitis A, AB, IgM, hepatitis B core antibody, IgM, hepatitis B surface antigen, IgM, hepatitis C, AB 7-mL red-topped tube
Lipid Panel (LIPID PN)Cholesterol, HDL, triglycerides (LDL and CHO/HDL ratio included, as calculated values)
Sophisticated automated instrumentation◦ makes it possible to conduct a wide variety
of chemical tests ◦ on a single sample of blood ◦ and to report results in a timely manner.
Numerical results may be reported with low, high, panic, toxic, or D (ie, fails Delta check) comments along with normal reference range.
◦ Computerized interfaces allow direct transmission of results between laboratory and clinical settings.
◦ Hard-copy” printouts can then become a permanent part of the health care record.
EnzymesEnzymesAll known enzymes are proteinsEnzymes are simply biological
catalysts, made (mostly) of proteinMany enzymes require the presence
of other compounds - cofactors - before their catalytic activity can be exerted
This entire active complex is referred to as the holoenzyme;
i.e., apoenzyme (protein portion) plus the cofactor (coenzyme,
prosthetic group or metal-ion-activator) is called the holoenzyme.
Apoenzyme + Cofactor =
Holoenzyme
Specificity of EnzymesSpecificity of EnzymesOne of the properties of enzymes
that makes them so important as diagnostic and research tools is the specificity they exhibit relative to the reactions they catalyze.
A few enzymes exhibit absolute specificity; that is, they will catalyze only one particular reaction.
Other enzymes will be specific for a
particular type of chemical bond or functional group.
In general, there are four distinct types of specificity:◦ 1. Absolute specificity - the enzyme will catalyze
only one reaction.
◦ 2. Group specificity - the enzyme will act only on molecules that have specific functional groups, such as amino, phosphate and methyl groups.
◦ 3. Linkage specificity - the enzyme will act on a particular type of chemical bond
regardless of the rest of the molecular structure.
◦ 4. Stereochemical specificity - the enzyme will act on a particular steric or optical isomer.
Enzymes are classified based on what they do to their substrates, according to the Enzyme Commission (EC) classification
Oxidoreductases transfer electrons (often as hydride ions H−).
Transferases transfer chemical groups between molecules.
Hydrolases add or remove H2O from molecules.
Lyases manipulate double bonds by elimination reactions.
Isomerases transfer chemical groups within molecules.
Ligases condense C-{S/N/C/O} bonds using energy from ATP.
Enzyme Classification Enzyme Classification Addition or removal of water
◦ Hydrolases - these include esterases, carbohydrases, nucleases, deaminases, amidases, and proteases
◦ Hydrases such as fumarase, enolase, aconitase and carbonic anhydrase
Transfer of electrons ◦ Oxidases ◦ Dehydrogenases
Transfer of a radical ◦ Transglycosidases - of monosaccharides ◦ Transphosphorylases and phosphomutases - of a phosphate group ◦ Transaminases - of amino group ◦ Transmethylases - of a methyl group ◦ Transacetylases - of an acetyl group
Splitting or forming a C-C bond ◦ Desmolases
Changing geometry or structure of a molecule ◦ Isomerases
Joining two molecules through hydrolysis of pyrophosphate bond in ATP or other tri-phosphate ◦ Ligases
Enzyme KineticsEnzyme KineticsEnzymes are catalysts and increase the
speed of a chemical reaction without themselves undergoing any permanent chemical change.
They are neither used up in the reaction nor do they appear as reaction products.
The basic enzymatic reaction can be represented as follows:
E + S ⇌ ES → E + P
where E represents the enzyme catalyzing the reaction, S the substrate, the substance being changed, and P the product of the reaction
Aspartate Transaminase Aspartate Transaminase (Aminotransferase, AST); Serum (Aminotransferase, AST); Serum Glutamic-Oxaloacetic Transaminase Glutamic-Oxaloacetic Transaminase (SGOT)(SGOT)decreasing concentrations of AST found in the
heart, liver, skeletal muscle, kidney, brain, pancreas, spleen, and lungs.
is released into the circulation following injury or death of cells. Any disease that causes change in these highly metabolic tissues will result in a rise in AST levels.
amount of AST in the blood is directly related to the number of damaged cells and the amount of time that passes between injury to the tissue and the test.
Following severe cell damage, the blood AST level will rise in 12 hours and remain elevated for about 5 days.
evaluate liver and heart disease.
AST Normal Values Men: 14–20 U/L Women: 10–36 U/L Newborns: 47–150 U/L Children: 9–80 U/L
SampleSampleObtain a 5-mL venous sample
(red-topped tube). Serum is used. Observe standard precautions. Place specimen in a biohazard
bagAvoid hemolysis.
Clinical ImplicationsClinical Implications ASTAST
Increased AST levels occur in ◦MI.
In MI, may be increased to 4 to 10 times the normalpeak in 24 hours and returns to normal by post-MI day 3
to 7. Secondary rises in AST levels suggest recurrence of MI.
a. liver diseases (10–100 times normal). a. Acute/chronic hepatitis (ALT > AST)
b. Active cirrhosis (drug induced; alcohol induced: AST > ALT) c. Infectious mononucleosis d. Hepatic necrosis and metastasis e. Primary or metastatic carcinoma f. Alcoholic hepatitis
Decreased AST levels occur in the following conditions:
a. Azotemia b. Chronic renal dialysis c. Vitamin B6 deficiency
Alanine Aminotransferase Alanine Aminotransferase (Aminotransferase, ALT); Serum Glutamic-(Aminotransferase, ALT); Serum Glutamic-Pyruvic Transaminase (SGPT)Pyruvic Transaminase (SGPT)
High concentration in liver, and low in heart, muscle, and kidney.
primarily used to diagnose liver disease monitor treatment for hepatitismore sensitive in the detection of liver
disease than in biliary obstruction. ALT also differentiates between
hemolytic jaundice and jaundice due to liver disease.
Normal Adults: ◦ Males: 10–40 U/L ◦ Females: 7–35 U/L ◦ Newborns: 13–45 U/L
ALT values slightly higher in males and black persons.
Increased ALT levels Hepatocellular disease (moderate to high
increase) Alcoholic cirrhosis (mild increase)Metastatic liver tumor (mild increase) Obstructive jaundice or biliary obstruction (mild
increase) Viral, infectious, or toxic hepatitis (30–50 times
normal)Infectious mononucleosisPancreatitis (mild increase)Myocardial infarction, heart failurePolymyositisSevere burns Trauma to striated muscleSevere shock
AST/ALT comparison: ◦AST level is always increased in acute
MI,◦ALT level does not always increase
unless there is also liver damage.◦ALT is increased more than AST in
acute extrahepatic biliary obstruction.◦ALT more specific than AST for liver
disease◦AST is more sensitive to alcoholic liver
disease.
Alkaline Phosphatase Alkaline Phosphatase (ALP)(ALP)
enzyme originating mainly in bone, liver, and placenta,
functions best at a pH of 9. levels are age and gender dependent.
◦ Postpuberty ALP is mainly of liver origin.used as an index of liver and bone disease
◦ when correlated with other clinical findings. In bone disease,
◦ level rises in proportion to osteoblastic activity and the deposit of calcium in the bones.
In liver disease, ◦ level rises when excretion is impaired as a result of
obstruction in the biliary tract.◦ Used alone, alkaline phosphatase may be misleading
Elevated levels of ALP in liver disease (correlated with abnormal liver function tests) occur in the following conditions: ◦ Obstructive jaundice (gallstones obstructing
major biliary ducts; accompanying elevated bilirubin)
◦ Space-occupying lesions of the liver such as cancer (hepatic carcinoma) and malignancy with liver metastasis
◦ Hepatocellular cirrhosis ◦ Biliary cirrhosis ◦ Intrahepatic and extrahepatic cholestasis ◦ Hepatitis, infectious mononucleosis,
cytomegalovirus◦ Diabetes mellitus (causes increased synthesis),
diabetic hepatic lipidosis◦ Chronic alcohol ingestion
Bone disease and elevated ALP levels occur in the following conditions: ◦ Paget’s disease (osteitis deformans;
levels 10 to 25 times normal) ◦Metastatic bone tumor ◦Osteogenic sarcoma ◦Osteomalacia (elevated levels help
differentiate between osteomalacia and osteoporosis, in which there is no elevation)
Other diseases involving elevated ALP levels include the following:
Hyperparathyroidism (accompanied by hypercalcemia), hyperthyroidism
Pulmonary and myocardial infarctions
Hodgkin’s disease Cancer of lung or pancreas Ulcerative colitis, peptic ulcerSarcoidosis Perforation of bowel (acute
infarction)
Interfering FactorsInterfering FactorsPhysiologically high levels of ALP ◦Young children, pregnant women, and
postmenopausal women have; slightly increased in older persons.
• After IV administration of albumin, there is sometimes a marked increase in ALP for several days.
• ALP levels increase at room temperature and in refrigerated storage. Testing should be done the same day.
• ALP levels decrease if blood is anticoagulated• ALP levels increase after fatty meals.(fasting
specimen)
Gamma Gamma Glutamyltransferase Glutamyltransferase (gamma-Glutamyl (gamma-Glutamyl Transpeptidase, GGT, GT)Transpeptidase, GGT, GT)present mainly in the liver,
kidney, and pancreas. kidney has the highest level of
this enzyme,but the liver is considered the source of normal serum activity.
GT has no origin in bone or placenta.
GGT, GTGGT, GTused to determine liver cell dysfunction
and to detect alcohol-induced liver disease.
very sensitive to the amount of alcohol consumed ◦monitor cessation or reduction of alcohol
consumptionactivity is elevated in all forms of liver
disease. much more sensitive than either the
AP, SGOT, SGPT in detecting obstructive jaundice, cholangitis, and cholecystitis.
NormalMen: 7–47 U/L Women: 5–25 U/L Values are higher in newborns
and in the first 3–6 months. Values in adult males are 25%
higher than in females. Serum is used.
Increased GT levels associated with Liver diseases
Hepatitis (acute and chronic) Cirrhosis (obstructive and familial) Liver metastasis and carcinoma Cholestasis (especially during or following
pregnancy) Chronic alcoholic liver disease Infectious mononucleosis
GT levels are also increased in the following conditions:◦ Pancreatitis ◦Carcinoma of prostate ◦Carcinoma of breast and lung◦ Systemic lupus erythematosu◦Glycogen storage disease
In MI, GT is usually normal. if increased, it occurs about 4 days after MI and
probably implies liver damage secondary to cardiac insufficiency.
Increased in Hyperthyroidism,decreased in hypothyroidism.
GT values are normal in: bone disorders, bone growth, pregnancy, skeletal muscle disease, strenuous exercise, renal failure. Children and adolescents
GGTGGTInterpret test results and monitor
as appropriate for liver, pancreatic, or thyroid disease and cancer recurrence.
Lactate Dehydrogenase Lactate Dehydrogenase (LD, LDH)(LD, LDH)intracellular enzyme, widely
distributed in the tissues of the body:◦kidney, heart, skeletal muscle, brain,
liver, and lungs. Increases indicate cellular death
and leakage of the enzyme from the cell.
Lactate Dehydrogenase Lactate Dehydrogenase (LD, LDH)(LD, LDH)elevated levels of LDH are
nonspecific, useful in confirming pulmonary
infarction also helpful in the differential
diagnosis of muscular dystrophy and pernicious anemia
More specific findings by breaking down the LDH into its five isoenzymes. (When LD values are reported or quoted, total LDH is meant.)
Normal Normal
Newborn: 160–450 U/L • Children: 60–170 U/L • Adults: 140–280 U/L
- Serum is used. - Avoid hemolysis in obtaining
blood sample.
Increased LDH (LD)Increased LDH (LD) High levels within 36 to 55 hours after
MI and continue longer than elevations of SGOT or CPK (3–10 days). Differential diagnosis of acute MI may be accomplished without LDH isoenzymes.
In pulmonary infarction, within 24 hours of pain onset. The pattern of normal SGOT and elevated LDH that levels off 1 to 2 days after an episode of chest pain is indicative of pulmonary infarction.
Elevated levels of LDH are also observed: Congestive heart failure Liver diseases (eg, cirrhosis, alcoholism, acute viral
hepatitis) Malignant neoplasms, cancer, leukemias, lymphomaHypothyroidism Lung diseases Skeletal muscle diseases (muscular dystrophy), muscular
damage Megaloblastic and pernicious anemias, hemolytic anemia,
sickle cell disease Delirium tremens, seizures Shock, hypoxia, hypotension Hyperthermia Renal infarctCNS diseasesAcute pancreatitisFractures, other trauma including head injury
Interfering FactorsInterfering Factors Note: Decreased LDH levels are associated
with a good response to cancer therapy.Strenuous exercise and the muscular
exertion involved in childbirth cause increased LDH levels.
Skin diseases can cause falsely increased LDH levels.
Hemolysis of red blood cells due to freezing, heating, or shaking the blood sample will cause falsely increased LDH levels
Clinical Alert LDH is found in nearly every tissue of the body; therefore, elevated levels are of limited diagnostic value by themselves. Differential diagnoses may be accomplished with LD isoenzyme determination.
(LDH, LD) Isoenzymes (LDH, LD) Isoenzymes (Electrophoresis)(Electrophoresis)The origins of the LDH
isoenzymes are as follow: LD1 and LD2 are present in
cardiac tissue and erythrocytes; LD3 originates mainly from lung,
spleen, pancreas, and placenta; and LD4 and LD5 originate from
skeletal muscle and liver.
The five isoenzyme fractions of LDH show different patterns in various disorders.
Abnormalities in the pattern suggest which tissues have been damaged.
This test is useful in the differential diagnosis of
acute MI, megaloblastic anemia (eg, folate deficiency,
pernicious anemia), hemolytic anemia
◦ These entities are characterized by LD1 increases, often with LD1:LD2 inversion (flip).
Normal LD1: 17%–27% of total or 0.17–0.27LD2: 29%–39% of total or 0.29–0.39 LD3: 19%–27% of total or 0.19–0.27 LD4: 8%–16% of total or 0.08–0.16 LD5: 6%–16% of total or 0.06–0.16
Obtain a 5-mL venous blood sample (red-topped tube). Serum is needed.
2. Avoid hemolysis. 3. Observe standard precautions. Place
specimen in a biohazard bag. Be aware that serial determinations may
be ordered (3 consecutive days).
Clinical Alert LDH isoenzymes should be interpreted in light of clinical findings.
Disease LD1 LD2 LD3 LD4 LD5 Myocardial infarction X X Pulmonary infarction X X Congestive heart failure X X Viral hepatitis X X Toxic hepatitis X X
Leukemia,granulocytic X X Pancreatitis X X Carcinomatosis (extensive) X X Megaloblastic anemia X X Hemolytic anemia X X Muscular dystrophy X X
Cardiac Troponin T (cTnT); Cardiac Troponin T (cTnT); Troponin I (cTnI)Troponin I (cTnI)
unique to the heart muscle and is highly concentrated in cardiomyocytes.
high degree of cardiac specificity. released with very small areas of
myocardial damage as early as 1 to 3 hours after injury, levels return to normal within 5 to
7 days.
Troponin I remains increased longer than CK-MB and is more cardiac specific.
Troponin T is more sensitive but less specific, being positive with angina at rest.
the most important addition to the clinical assessment of cardiac injury.
Cardiac troponin is the preferred test to diagnose MI.
used in the early diagnosis of small myocardial infarcts that are undetectable by conventional diagnostic methods.
also used later in the course of MI because they remain elevated for 5 to 7 days after injury.
serial sampling 0, 4, 8, and 12 hours after chest pains may be ordered to rule out acute MI.
Cardiac MarkersCardiac Markers
markers Initial Elevation
Time of peak Back to Nl
CK-MB 4-8 hr 12-24 hr 72-96 hr
Myoglobin 2-4 hr 8-10 hr 24 hr
Troponin I 4-6 hr 12 h 3-10 days
Normal Negative (Qualitative) Troponin I: <0.35 ng/mL Total CK: 0–120 ng/mL CK-MB: 0–3 ng/mL Myoglobin: <55 ng/mL Troponin: <0.4 ng/mL
Positive or elevated cardiac troponin I levels indicate:
Small infarcts; increases remain for 5 to 7 days.
Myocardial injury during surgery
Interfering FactorsInterfering Factors Cardiac troponin I levels may be
increased in chronic muscle or renal disease and trauma.
Levels are not affected by orthopedic or lung surgery.
Creatine Phosphokinase (CPK); Creatine Creatine Phosphokinase (CPK); Creatine Kinase (CK); CPK and CK IsoenzymesKinase (CK); CPK and CK Isoenzymes
higher concentrations in heart and skeletal muscles smaller brain tissue. used as a specific index of injury to myocardium and muscle. three isoenzymes: MM, BB, and MB Skeletal muscle contains primarily MM; cardiac muscle contains primarily MM and MB; and brain tissue, GI system, and genitourinary tract contain
primarily BB. Normal CK levels are virtually 100% MM isoenzyme. A slight increase in total CPK is reflected from elevated BB from
CNS injury. CPK isoenzyme studies help distinguish whether the CPK
originated from the heart (MB) or the skeletal muscle (MM).
The CK (CPK) testThe CK (CPK) testused in the diagnosis of MI reliable measure of skeletal and
inflammatory muscle diseases. helpful in recognizing muscular dystrophy
before clinical signs appear. CK levels may rise significantly with CNS
disorders such as Reye’s syndrome. CK isoenzymes may be helpful in making a
differential diagnosis. Elevation of MB, the cardiac isoenzyme,
provides a more definitive indication of myocardial cell damage than total CK alone.
MM isoenzyme is an indicator of skeletal muscle damage.
CPKCPKNormal Men: 38–174 U/L Women: 26–140 U/L Infants: 2–3 times adult values
Increased CK/CPK levelsIncreased CK/CPK levels occur in the followingoccur in the followingAcute MI Severe myocarditis After open heart surgeryCardioversion (cardiac
defibrillation)Myocarditis
Other diseases and procedures that cause increased Other diseases and procedures that cause increased CK/CPK levels include the following:CK/CPK levels include the following:
Acute cerebrovascular disease Progressive muscular dystrophy (levels may reach 20–200
times normal), Duchenne’s muscular dystrophy, female carriers of muscular dystrophy
Dermatomyositis and polymyositis Delirium tremens and chronic alcoholism Electric shock, electromyography Malignant hyperthermia Reye’s syndrome Convulsions, ischemia, or subarachnoid hemorrhage Last weeks of pregnancy and during childbirth Hypothyroidism Acute psychosis CNS trauma, extensive brain infarction Neoplasms of prostate, bladder, or GI tract Rhabdomyolysis with cocaine intoxication
Elevated MB (CKElevated MB (CK22) ) isoenzyme levelsisoenzyme levels occur occur
in the following conditions:in the following conditions: Myocardial infarct Myocardial ischemia, angina pectoris Duchenne’s muscular dystrophy Subarachnoid hemorrhage Reye’s syndrome Muscle trauma, surgery (postoperative) Circulatory failure and shock Infections of heart—myocarditis Chronic renal failure Malignant hyperthermia, hypothermia CO poisoning Polymyositis Myoglobulinemia
Interfering FactorsInterfering FactorsStrenuous exercise, weight lifting, and
surgical procedures that damage skeletal muscle may cause increased levels
Alcohol and other drugs of abuse increase CK levels.
Athletes have a higher CK value because of greater muscle mass
Multiple IM injections may cause increased Many drugs may cause increased CK levels
Childbirth may cause increased CK levels. Hemolysis of blood sample causes
increased CK levels.
Angiotensin-Converting Angiotensin-Converting Enzyme (ACE)Enzyme (ACE)catalyzes the conversion of
angiotensin I to the vasoactive peptide angiotensin II.
Angiotensin I is concentrated in the proximal tubules.
This test is used primarily to evaluate the severity and activity of sarcoidosis.
Serial determinations may be helpful in following the clinical course of the disease with steroid treatment.
It is also used in the investigation of Gaucher’s disease.
ACE: 8–53 U/LObtain a 5-mL venous blood
sample (red-topped tube). Serum or heparinized plasma is used.
Freeze specimen if test is not performed immediately.
Increased ACE levelsIncreased ACE levelsSarcoidosis Gaucher’s disease Leprosy Acute and chronic bronchitis Connective tissue diseases Amyloidosis Pulmonary fibrosis Fungal diseases and histoplasmosis Untreated hyperthyroidism Diabetes mellitus Psoriasis
Interfering FactorsInterfering FactorsThis test should not be done in persons
<20 years of age because they normally have a very high level of ACE.
About 5% of the normal adult population has elevated ACE levels.
ACE is inhibited by EDTA anticoagulant. Some antihypertensives may cause low
ACE values.
AmylaseAmylaseenzyme that changes starch to
sugar, is produced in the salivary
(parotid) glands and pancreas; much lower activities are
present in the ovaries, intestines, and skeletal muscle.
If there is an inflammation of the pancreas or salivary glands, much amylase enters the blood.
LipaseLipaseglycoprotein that changes fats to fatty
acids and glycerol. The pancreas is the major source of
this enzyme. Lipase appears in the blood following
pancreatic damage at the same time amylase appears (or slightly later)
but remains elevated much longer than amylase (7 to 10 days).
Amylase and lipase ◦tests are used to diagnose and monitor
treatment of acute pancreatitis and to differentiate pancreatitis from other
acute abdominal disorders
◦(80% of patients with acute pancreatitis will have elevated amylase and lipase levels;
Lipase assay provides better sensitivity and specificity
Normal
◦Amylase • Newborns: 6–65 U/L • Adults: 25–125 U/L • Elderly persons (>60 years): 24–151
U/L
◦Lipase • Adults: 10–140 U/L • Elderly persons (>60 years): 18–180
U/LChildren up to 2 years of age have virtually no pancreatic amylase.
Obtain a 5-mL venous blood sample (red-topped tube). Serum is used. (EDTA, citrate, and oxalate anticoagulant interfere with lipase testing.)
Clinical ImplicationsClinical ImplicationsGreatly increased amylase levels occur in acute
pancreatitis early in the course of the disease. The increase begins in 3 to 6 hours after the onset of pain.
Increased amylase levels also occur in the following conditions: ◦ Chronic pancreatitis, ◦ pancreatic trauma, ◦ pancreatic carcinoma, obstruction of pancreatic duct ◦ Partial gastrectomy ◦ Acute appendicitis, peritonitis ◦ Perforated peptic ulcer ◦ Cerebral trauma, shock ◦ Obstruction or inflammation of salivary duct or gland and
mumps ◦ Intestinal obstruction with strangulation ◦ Ruptured tubal pregnancy and ectopic pregnancy ◦ Ruptured aortic aneurysm ◦ Macroamylasemia
Decreased amylase levelsDecreased amylase levelsPancreatic insufficiency Hepatitis, severe liver disease Advanced cystic fibrosis Pancreatectomy
Elevated lipase levelsElevated lipase levelsoccur in pancreatic disorders ◦(eg, pancreatitis, alcoholic and nonalcoholic;
pancreatic carcinoma). Increased lipase values also are
associated with the following conditions: Cholecystitis Hemodialysis Strangulated or infarcted bowel Peritonitis e. Primary biliary cirrhosis Chronic renal failure
Serum lipase levels are normal in patients with elevated amylase who have :◦peptic ulcer,◦ salivary adenitis, ◦inflammatory bowel disease,◦ intestinal obstruction
Interfering FactorsInterfering Factors
Amylase Anticoagulated blood gives lower
results. Do not use EDTA, citrate, or oxalate.
Lipemic serum interferes with test. Increased levels are found in alcoholic
patients and pregnant women and in diabetic ketoacidosis.
Many drugs can interfere with this test
Interfering FactorsInterfering FactorsLipase EDTA anticoagulant interferes
with test. Lipase is increased in about
50% of patients with chronic renal failure
Lipase increases in patients undergoing hemodialysis.
Many drugs can affect outcomes.
Homocysteine (tHcy) Homocysteine (tHcy) Amino acid resulting from the
synthesis of cysteine from methionine and enzyme reaction of cobalamin and folate.
homocystinemia homocystinemia associated withassociated with-Increased risk for vascular disease-Increased risk for venous thrombosis -has a direct toxic effect on
endothelium-Elevated in folic acid deficiency and
B12 deficiency
-Increased risk for pregnancy complications and neural tube defects
This test measures the blood plasma level of homocysteine.
It is useful◦ diagnosing individuals with potential
increased risk factors for coronary artery disease and thromboses,
◦ providing a functional assay for folic acid deficiency,
◦ diagnosing homocystinemia. Homocysteine is retained by persons with reduced renal function.
Clinical ImplicationsClinical ImplicationsIncreased or elevated
homocysteine levels occur in the following conditions:◦ Folic acid deficiency ◦Abnormal vitamin B12 metabolism
and deficiency ◦Homocystinuria
The End