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SECOND SEM 3rd YEAR > CC2 Lab Enzymology 1 & 2 > Flashcards

CC2 Lab Enzymology 1 & 2 Flashcards

1
Q

reacts at a designated time

A

Fixed time

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2
Q

multiple measurements of absorbance changes
are made during the reaction

A

Kinetic assay

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3
Q

An enzyme important in the regeneration of adenosine triphosphate

A

Creatine Kinase - “ATP-Creatine-N Phosphotransferase”

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4
Q

Predominantly found in skeletal muscles, heart muscles, brain tissues

A

Creatine Kinase - “ATP-Creatine-N Phosphotransferase”

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5
Q

Creatine Kinase is most commonly used in the diagnosis of ___,___ and ____.

A

acute myocardial infarction, muscular dystrophy, and central nervous system disorders

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6
Q

Abundant in Cardiac and Skeletal muscles

A

CK-MM - “Muscle Type”, “CK-3”

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7
Q

Major isoenzyme in sera of healthy people

A

CK-MM - “Muscle Type”, “CK-3”

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8
Q

Normally found in neonatal sera (rare in adult serum)

A

CK-BB - “Brain Type”, “CK-1”

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9
Q

Elevated in brain injury and carcinomas

A

CK-BB - “Brain Type”, “CK-1”

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10
Q

With significant amount in the heart

A

CK-MB - “hybrid type”, “CK-2”

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11
Q

Most specific for Myocardial damage (AMI)

A

CK-MB - “hybrid type”, “CK-2”

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12
Q

Falsely elevated in hemolysis

A

CK-MB - “hybrid type”, “CK-2”

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13
Q

CK-MB - “hybrid type”, “CK-2”

Elevates in ______
Peaks at ______
Normalize in __________

A

Elevates in 4-8 hours
Peaks at 12-24 hours
Normalize in 48-72 hours

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14
Q

Common in older women

A

Macro-CK

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15
Q

Migrates middle of MM and MB

A

Macro-CK

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16
Q

Migrates cathodal to CK-MM

A

Mitochondrial CK (CK-Mi)

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17
Q

Indicates severe illness

A

Mitochondrial CK (CK-Mi)

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18
Q

Test Methods under CK

A
  1. Forward - Tanzer and Gilvarg Assay
    - pH: 9.0
    - Absorbance: 340nm
  2. Reverse - Oliver Rosalki
    - pH: 6.8
    - Absorbance: 340 nm
  3. Electrophoresis
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19
Q

proteins within cells

A

Enzymes

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20
Q

General Properties of Enzymes:

A

Active Site: Water Free
Allosteric site: Cavity other than the active site

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21
Q

non-protein that must bond to a particular enzyme before a reaction occurs

A

Cofactors

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22
Q

Enzyme Storage

A

-20C

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23
Q

A transferase that hastens the interconversion of lactic acid and pyruvic acid

A

Lactate Dehydrogenase - L-lactate: NAD oxidoreductase

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24
Q

Highest levels on Lactate Dehydrogenase are detected in ____ & ______

A

pernicious anemia and hemolytic disorders

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25
Q

Other disease associated with Lactate Dehydrogenase elevations are _____, ______, _______, ________.

A

hepatic disorders, acute myocardial infarction, pulmonary infarct, acute lymphoblastic leukemia

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26
Q

Isoenzymes: LDH1 (HHHH)

A

Heart, RBC, Kidneys

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27
Q

Isoenzymes: LDH2 (HHHM)

A

Major isoenzyme in healthy people
Most abundant and heat stable

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28
Q

Isoenzymes: LDH3 (HHMM)

A

lungs, pancreas, spleen, lymphocytes

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29
Q

Isoenzymes: LDH4 (HMMM)

A

skeletal muscle, liver, intestine

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30
Q

Isoenzyme: LDH5 (MMMM)

A

liver, skeletal muscle, intestine

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31
Q

Isoenzymes: LDH6

A

an arterioslcerotic Cardiovascular failure marker

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32
Q

LDH Clinical Significance

A
  1. Myocardial Infarction
    - Elevates at 12-24 hours after onset
    - Peaks at 48-72 hours
    - Remains elevated for 10 days
  2. Hepatitis
  3. Hemolysis
  4. Lung and muscle disorders
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33
Q

LDH Methods

A
  1. Wacker method - Forward or direct
    - pH: 8.8
    - Absorbance: 340 nm
  2. Wroblewski Ladue - Reverse or indirect
    - pH: 7.2
    - Abrosbanc: 340 nm
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34
Q

Transport and stores oxygen to intracellular respiratory enzymes of contractile cells (With high affinity to O2)

A

Myoglobin

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35
Q

Found in myocardium and with greater cardiac specificity

A

Troponin I

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36
Q

A Heart Failure Biomarker

A

Brain-type natriuretic peptide

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37
Q

Derived from a pro-hormone, “Pro-BNP”

A

Brain-type natriuretic peptide

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38
Q

Myoglobin:
Elevates _______
Peaks at ______
Normalizes _________

A

Elevates 2-3 hours after onset
Peaks at 8-12 hours
Normalizes 18-30 hours

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39
Q

Troponin I:
Elevates _____
Peaks at ______
Normalize in ______

A

Elevates 3-6 hours after onset
Peaks at 12-18 hours after onset
Normalize in 6 days

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40
Q

Considered as the smallest enzyme

A

Amylase - “Alpha 1-4 Glucan 4 Glucohydrolase”

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41
Q

Amylase Activators

A

Calcium and Chloride

42
Q

Amylase Substrate

A

Starch or Glycogen

43
Q

Amylase Major sources:

A
  1. Acinar cells of the pancreas - releases Amylopsin
  2. Salivary glands - releases Ptyalin
44
Q

Amylase used for the breakdown of ___ & ___

A

Glycogen and Starch

45
Q

Amylase Clinical Significance

A
  1. Acute Pancreatitis - first to elevate
    - Elevates 2-12 hours after onset
    - Peaks at 24 hours
    - Normalizes in 3-5 days
  2. Intestinal obstruction
  3. Cholecystitis
  4. Acute appendicitis
46
Q

Amylase Methods: measures reducing sugar from starch breakdown

A

Saccharogenic

47
Q

Amylase Methods: also known as Iodometric method

A

Amyloclastic

48
Q

Amylase Methods: Measure amylase activity by following decrease in substrate concentration

A

Amyloclastic

49
Q

Indicator used of Amyloclastic

A

Iodide

50
Q

Amylase Methods: uses dye to check amylase activity

A

Chromogenic

51
Q

Amylase Methods: Follows breakdown of starch

A

Amyloclastic

52
Q

A single-chain glycoprotein with a molecular weight of 48 kDa

A

Lipase - Triacylglycerol acylhydrolase

53
Q

Lipase needs the presence of ____ & ____

A

Bile salts and colipase

54
Q

Lipase Function:

A

Hydrolyze glycerol esters of long-chain fatty acids

55
Q

Most lipase activity found in serum are usually from _______

A

the pancreas and some
are secreted by gastric and intestinal mucosa

56
Q

molecular weight of Lipase

A

48 kDa

57
Q

Lipase Clinical Significance

A
  1. Acute Pancreatitis
  2. Perforated or duodenal ulcer
  3. Intestinal obstruction
  4. Mesenteric vascular obstruction
58
Q

Lipase Reference Method

A

Cherry Crandal

59
Q

What substance is utilized on Cherry Crandal for hydrolysis

A

Olive oil

60
Q

Cherry Crandal indicator

A

Phenolphthalein

61
Q

Liberates inorganic phosphate from an organic esters with the concomitant production of alcohol

A

Alkaline phosphatase

62
Q

Alkaline phosphatase Also known as

A

Alkaline Orthophosphoric Monoester Phosphohydrolase

63
Q

Alkaline phosphatase requires __ & __ as activator

A

Magnesium and Manganese

64
Q

Alkaline phosphatase Major Sources:

A

Liver
Kidneys
Placenta
Intestine
Spleen
Bone

65
Q

Alkaline phosphatase Optimum pH

A

9.0-10.5

66
Q

Alkaline phosphatase Elevated in:

A

Osteoblastic activity in kids during growth
>50 years old
Pregnancy (16-18 weeks)

67
Q

Alkaline phosphatase Clinical Significance

A

Obstructive jaundice
Pregnancy
Paget’s disease
Rickets
Bone Cancer
Other bone disease

68
Q

Alkaline phosphatase Methods

A

Electrophoresis
Liver ALP
Bone ALP
Placental ALP
Intestinal ALP
Regan
Nagao

Heat Stability
Placental
Intestinal
Liver
Bone

Chemical Inhibition
Phenylalanine
3M Urea
L-leucine
Levamisole

69
Q

Give the substrate and the product of Bodansky, Shinowara, Jones, Reinhart

A

Substrate: B-glycero phosphate
Product: Inorganic Phosphate Glycerol

70
Q

Give the substrate and the product of King Armstrong

A

Substrate: Phenylphosphate
Product: Phenol

71
Q

Give the substrate and the product of Bessy, Lowry, Brock, Bowers, Mccomb

A

Substrate: P-nitrophenyl phosphate
Product: P-nitrophenol

72
Q

Transfer of amino group between aspartate and alpha-ketoacids resulting to Oxaloacetate and Glutamate

A

Aspartate aminotransferase

73
Q

Aspartate aminotransferase also known as

A

Serum Glutamic Oxaloacetic Transaminase

74
Q

Aspartate aminotransferase major & other source

A

Major:
Liver
Cardiac Tissue
Skeletal Muscle

Other Source:
Kidneys
Pancreas
RBCs

75
Q

Aspartate aminotransferase Significance:

A

Hepatocellular disorders (Hepatitis, Cirrhosis, Bile duct obstruction, Hepatic cancer)
Skeletal muscle injury
Gangrene
Myocarditis
Reye’s syndrome
AMI (Acute Myocardial Infarction)
Elevates 6-8 hours after onset
Peaks at 24 hours
Normalize in 5 days

76
Q

Aspartate aminotransferase methods

A
  1. Karmen method
    utilizes Malate dehydrogenase to monitor change in absorbance at 340nm
    pH: 7.3-7.8
  2. Reitman Frankel
77
Q

Transfer of amino group from alanine to alpha-ketoglutarate

A

Alanine aminotransferase

78
Q

Alanine aminotransferase also known as

A

Serum Glutamic Pyruvic Transaminase

79
Q

Alanine aminotransferase Abundant in the

A

liver

80
Q

Alanine aminotransferase other source

A

Kidney
Pancreas
RBCs
Heart
Skeletal Muscle
Lungs

81
Q

Alanine aminotransferase needs this vitamin as coenzyme

A

vitamin B6

82
Q

Alanine aminotransferase Significance:

A

Elevated in Hepatic Disorders
Monitor course of hepatitis treatment
Used to screen blood donors

83
Q

Alanine aminotransferase METHODS

A

Coupled Enzymatic Reaction
utilizes LDH to monitor change in absorbance at 340nm
pH: 7.3-7.8

84
Q

Principle of Coupled Enzymatic Reaction under ALT Method

A

Alanine + alpha ketoglutarate —ALT—> Pyruvate + glutamate
Pyruvate + NADH + H+ —-LDH—-> Lactate + NAD+

85
Q

Catalyzes the transfer or glutamyl groups between peptides through linkage at a gamma carboxyl group

A

gamma glutamyl transferase

86
Q

gamma glutamyl transferase also known as

A

Gamma glutamyl transpeptidase

87
Q

gamma glutamyl transferase main source

A

Hepatic Cells
Kidneys
Prostate
Pancreas
Brain

88
Q

gamma glutamyl transferase sensitive indicator of

A

alcoholism

89
Q

gamma glutamyl transferase Significance:

A

Hepatic disorders
Alcoholism
Drug overdose

90
Q

gamma glutamyl transferase method

A

Spectrophotometric method

91
Q

Spectrophotometric principle under ggt method

A

Gamma glutamyl-p-nitroaniline ——> p-nitroaniline

92
Q

the absorbance of Spectrophotometric method is measured at

A

405nm

93
Q

Catalyzes the hydrolysis of most ribonucleoside 5’-monophosphate and deoxynucleoside 5’-monophosphate to the corresponding nucleoside and orthophosphate

A

5’nucleotidase

94
Q

5’nucleotidase also known as

A

Phosphoric monoester hydrolase

95
Q

5’nucleotidase main source

A

Liver

96
Q

5’nucleotidase is a Marker of

A

Hepatobillary disease and Infiltrative lesions of the liver

97
Q

Catalyzes the hydrolysis of several orthophosphoric monoesters to yield the corresponding alcohol and inorganic phosphate

A

acid phosphatase

98
Q

acid phosphatase also known as

A

Acid Orthophosphoric Monoester Phosphohydrolase

99
Q

acid phosphatase main source

A

Prostate
Liver
Kidneys
RBCs
Platelets
Osteoclastic Cells

100
Q

acid phosphatase optimum pH

A

4.5-7.0

101
Q

acid phosphatase Clinical Significance:

A

Prostatic
marker for prostatic carcinoma
Prostatic hypertrophy
Non-prostatic: Gaucher’s disease, Neimann-pick disease
Osteoclastic - hyperthyroidism, Paget’s disease, Multiple myeloma
Hematologic
Granulocytic leukemia
chronic lymphocytic leukemia
plasma cell leukemia
hairy cell leukemia

102
Q

acid phosphatase method

A

Bodansky method
King-Armstrong
Bessey-Lowry-Brock
Roy and Hillman
Babson, Read and Philips

SECOND SEM 3rd YEAR (38 decks)

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