Clinical Enzymology Liver Transfera

Question 1

Liver transferases enzyme

Answer 1

AST, ALT, ALP, GGT

Question 2

Alternative name for AST

Answer 2

Serum glutamic oxaloacetic transaminase (SGOT)

Question 3

Substrate for AST

Answer 3

Aspartate

Question 4

Reaction of AST

Answer 4

Exchange of amino group for oxaloacetate

Question 5

Distribution of AST

Answer 5

Liver, Heart, Skeletal Muscle

Question 6

Diagnostic use of AST

Answer 6

Increased in acute hepatocellular disorders, circulatory collapse, myocardial infarction

Question 7

Moderate increase in AST

Answer 7

Muscular dystrophy, hepatic tumor, biliary obstruction, CHF, cardiac arrhythmia

Question 8

Slight increase in AST

Answer 8

Cirrhosis, pericarditis, pulmonary infarction, cerebrovascular accident

Question 9

Reference value for AST

Answer 9

5-35 IU/L or <36 IU/L

Question 10

Isoenzymes of AST

Answer 10

Mitochondrial and cytoplasmic

Question 11

Increase in cytoplasmic AST

Answer 11

Acute hepatocellular disorders (AHCDs)

Question 12

Increase in mitochondrial AST

Answer 12

Hepatic failure, alcoholic liver disease (fulminant Hf)

Question 13

Alternative name for ALT

Answer 13

Serum glutamic pyruvic transaminase (SGPT)

Question 14

Reaction for ALT

Answer 14

Alanine is converted to pyruvate

Question 15

Main purpose of ALT conversion

Answer 15

Amino acid metabolism and degradation (gluconeogenesis)

Question 16

Diagnostic value of ALT in acute hepatocellular disorders

Answer 16

De Ritis ratio <1

Question 17

Significance of De Ritis ratio in ALT

Answer 17

More specific, higher and sustained elevation (AST/ALT) - decreased <1

Question 18

Comparison of half-life for AST and ALT

Answer 18

ALT has a longer half-life than AST

Question 19

Distribution of ALT

Answer 19

Liver (more liver-specific)

Question 20

Reference value for ALT

Answer 20

7-45 IU/L

Question 21

Specimen consideration for AST and ALT

Answer 21

Avoid prolonged storage and hemolysis

Question 22

Methods for AST and ALT

Answer 22

Reitman-Frankel and Karmen method

Question 23

Reitman-Frankel method chemicals

Answer 23

2,4-dinitrophenylhydrazine and 0.4 N NaOH

Question 24

Reitman-Frankel coenzyme/cofactor

Answer 24

Vitamin B6 (pyridoxine/pyridoxal phosphate)

Question 25

Reitman-Frankel color product

Answer 25

Reddish brown at 505 nm

Question 26

Reitman-Frankel color developer

Answer 26

2,4-DNPH

Question 27

Method used for continuous monitoring of AST and ALT

Answer 27

Karmen method

Question 28

pH buffer range for AST and ALT continues monitoring

Answer 28

7.3 to 7.8

Question 29

Enzyme used for aspartate in AST method

Answer 29

Malate dehydrogenase

Question 30

Enzyme used for alanine in ALT method

Answer 30

Lactate dehydrogenase

Question 31

Product for AST in Karmen method

Answer 31

Malate and NAD (measured at decreased absorbance; 340 nm)

Question 32

Product for ALT in Karmen method

Answer 32

Lactate and NAD (measured at decreased absorbance; 340 nm)

Question 33

Activator for ALP

Answer 33

Magnesium (electrolyte)

Question 34

Main isoenzymes of ALP

Answer 34

Intestine, Liver, Bone, Placenta

Question 35

Small amounts of ALP found in

Answer 35

Kidney and Spleen

Question 36

Liver isoenzyme of ALP

Answer 36

Hepatobiliary

Question 37

Bone isoenzyme of ALP

Answer 37

Osteoblast

Question 38

Diagnostic significance of pronounced ALP elevation

Answer 38

Bile duct obstruction, biliary cirrhosis, Paget’s disease, osteogenic sarcoma, hyperparathyroidism

Question 39

Diagnostic significance of moderate ALP elevation

Answer 39

Granulomatous liver diseases, IM, metastatic bone tumors, rickets, osteomalacia

Question 40

Diagnostic significance of slight ALP elevation

Answer 40

Viral hepatitis, cirrhosis, healing bone fractures, growing children, pregnancy

Question 41

Reference range for ALP (Male)

Answer 41

53-128 IU/L

Question 42

Reference range for ALP (Female)

Answer 42

49-98 IU/L

Question 43

Reference range for ALP (Children)

Answer 43

54-369 IU

Question 44

Methods to avoid in ALP determination

Answer 44

CK, LD, LP

Question 45

Reference method for ALP determination

Answer 45

Bowers-McComb

Question 46

Bowers-McComb substrate for ALP

Answer 46

p-nitrophenylphosphate

Question 47

Product of Bowers-McComb method for ALP

Answer 47

p-nitrophenol (yellow)

Question 48

Substrate in Bessy, Lowey, and Brock/Bowers-McComb method

Answer 48

p-nitrophenylphosphate

Question 49

Measurable end product of Bessy, Lowey, and Brock/Bowers-McComb method

Answer 49

p-nitrophenol

Question 50

Substrate in Bodansky, Sinowara, Jones, Reinhart method

Answer 50

B-glycerophosphate

Question 51

Measurable endpoint in Shinowara method

Answer 51

Glycerol

Question 52

Substrate in King Armstrong method

Answer 52

Phenylphosphate

Question 53

Measurable end product in King Armstrong method

Answer 53

Phenol

Question 54

Substrate in Huggins and Talalay method

Answer 54

Phenolphthalein diphosphate

Question 55

Measurable end product in Huggins and Talalay method

Answer 55

Red phenolphthalein

Question 56

Substrate in Moss method

Answer 56

Alpha-napthylphosphate

Question 57

Measurable end product in Moss method

Answer 57

Alpha napthol

Question 58

Substrate in Klein Babson and Reed method

Answer 58

Buffered phenolphthalein phosphate

Question 59

Measurable end product in Klein Babson and Reed method

Answer 59

Phenolphthalein

Question 60

Electrophoresis migration pattern of ALP isoenzymes

Answer 60

I, P, B, L (Intestine, Placenta, Bone, Liver)

Question 61

Heat stability test for ALP isoenzymes

Answer 61

56°C for 10 minutes

Question 62

Heat stability pattern of ALP isoenzymes

Answer 62

P, I, L, B (Placenta most heat stable)

Question 63

Heat stability of Placental ALP

Answer 63

Resists heating at 65°C

Question 64

Heat stability of Bone ALP

Answer 64

<20% activity at 30 minutes

Question 65

Chemical inhibition by Phenylalanine

Answer 65

P, I (Placenta, Intestine, carcinoplacental)

Question 66

Chemical inhibition by Levamisole

Answer 66

B, L (Bone, Liver)

Question 67

Chemical inhibition by 3 molar urea

Answer 67

Bone

Question 68

Intestinal ALP characteristic

Answer 68

Increased after fatty meal, found in B or O secretor individuals

Question 69

Carcinoplacental abnormal isoenzyme

Answer 69

Regan

Question 70

Where Regan isoenzyme is detected

Answer 70

Lung, breast, ovarian, colon, and gynecologic cancers

Question 71

Carcinoplacental abnormal isoenzyme (Nagao)

Answer 71

Detected in carcinoma of pleural surfaces, pancreas, and bile duct

Question 72

Carcinoplacental abnormal isoenzyme (Kasahara)

Answer 72

Associated with GI and hepatic tumors

Question 73

Reference range for carcinoplacental isoenzymes

Answer 73

30-90 U/L

Question 74

Function of GGT

Answer 74

Transfer gamma-glutamyl amino acid residues (glutathione)

Question 75

Diagnostic use of GGT

Answer 75

Marker for hepatobiliary disorders, alcoholic liver disease, and microsomal induction by drugs and alcohol

Question 76

Use of GGT in hepatobiliary obstructions

Answer 76

Identifies source of increased ALP

Question 77

Popular use of GGT

Answer 77

Marker of chronic alcoholism

Question 78

Reference range for GGT (Male)

Answer 78

6-55 IU/L

Question 79

Reference range for GGT (Female)

Answer 79

5-38 IU/L

Question 80

Pre-analytical consideration for GGT

Answer 80

Always use a sample blank

Question 81

Effect of alcohol and drug abuse on GGT results

Answer 81

Increases GGT results

Question 82

Stability of GGT in serum

Answer 82

Stable up to 1 week if refrigerated

Question 83

Drugs that increase GGT

Answer 83

Warfarin, phenobarbital, phenytoin

Question 84

Szasz method substrate for GGT

Answer 84

Gamma-glutamyl-p-nitroanilide + glycylglycine

Question 85

Product of Szasz method for GGT

Answer 85

Gamma-glutamylglycylglycine + p-nitroanilide (yellow color)

Question 86

Measuring wavelength for Szasz method

Answer 86

420 nm