Enzymology Flashcards

1
Q

4 basic molecules:

A

Nucleic acids, lipids, carbohydrates, & proteins (have increase/large molecular weight)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

where substrate enters

A

Active Site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

water free

A

active site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

where an enzyme acts or bind for a reaction or product to happen

A

substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Cavity other than the active

A

allosteric site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

serves as catalyst (regulate or amplifies rate)

A

enzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

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

A

cofactors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

common cofactors for
enzymatic reactions:

A

Magnesium and Calcium Chloride

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

compete w/ the substrate to bind with active site

A

competitive

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

bind on the allosteric site (or anywhere except active site)

A

non-competitive

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

binds with enzyme-substrate complex

A

uncompetitive

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

same enzyme but different variant with a slight difference in structure can affect the function (different roles or can also be produced by different types of cells)

A

isoenzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

25-37C

A

enzymes are active

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

38-50C

A

denatured

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

60-65C

A

inactive

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

enzymology reaction that reacts at a designated time

A

fixed time

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

enzymology reactions that multiple measurement of absorbance changes are made during the reactions

A

kinetic assay

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

An enzyme important in the regeneration of adenosine triphosphate

A

CREATINE KINASE:
“ATP-Creatine-N-Phosphotransferase”

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What are enzymes?

A

Proteins within cells that act as catalysts for biochemical reactions.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What are the general properties of enzymes?

A

Enzymes have an active site where the substrate enters, and an allosteric site, which is a cavity other than the active site.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

What are the factors that affect enzymology?

A

Enzyme concentration, substrate concentration, cofactors, inhibitors, isoenzymes, temperature, and storage.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

What is the optimal temperature range for enzyme activity?

A

Enzymes are most active at temperatures between 25-37°C, denatured at 38-50°C, and inactive at 60-65°C.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

What is the purpose of storing enzymes at -20°C?

A

Enzymes are stored at -20°C for reagent and unprocessed samples.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

most commonly used in the diagnosis of acute myocardial infarction, muscular dystrophy, and central nervous system disorders?

A

Creatine kinase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

normally found in neonatal sera, low concentration in adults, elevated in brain injury and carcinomas

A

CK-BB (Brain Type, CK-1)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

most important isoenzyme for creatine kinase, significant amount in the heart, most specific for myocardial damage (AMI), (elevates in 4-8 hours, peaks at 12-24 hours, normalizes in 48-72 hours), falsely elevated in hemolysis

A

CK-MB (Hybrid Type, CK-2)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

abundant in cardiac and skeletal muscles, major activity in the heart, major isoenzyme in sera of healthy people

A

CK-MM (Muscle Type, CK-3)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

common in older women, migrates in the middle of MM and MB

A

Macro-CK

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

migrates cathodal to CK-MM, indicates severe illness.

A

Mitochondrial CK (CK-Mi)

30
Q

What are the methods used for creatine kinase measurement and their characteristics?

A

Forward - Tanzer and Gilvarg Assay: pH 9.0
Reverse - Oliver Rosalki: pH 6.8
— absorbance: 340 nm—-

Electrophoresis

31
Q

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

A

lactate dehydrogenase

32
Q

found in various tissue sources and composed of 4 peptide chains of 2 types: ‘M’ (A) and ‘H’ (B), both under separate genetic control.

A

lactate dehydrogenase

33
Q

Elevated levels are associated with several diseases, with the highest levels detected in pernicious anemia and hemolytic disorders

A

lactate dehydrogenase

34
Q

Other diseases associated with elevations are hepatic disorders, acute myocardial infarction, pulmonary infarct, and acute lymphoblastic leukemia.

A

lactate dehydrogenase

35
Q

what are the diseases associated in LDH

A

Elevated levels - pernicious anemia and hemolytic disorders

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

36
Q

Heart, RBC, Kidneys

A

LDH1 (HHHH)

37
Q

Major isoenzyme in healthy people, most abundant and heat-stable.

A

LDH2 (HHHM)

38
Q

Lungs, pancreas, spleen, lymphocytes

A

LDH3 (HHMM)

39
Q

Skeletal muscle, liver, intestine

A

LDH4 (HMMM) and LDH5 (MMMM)

40
Q

an arteriosclerotic cardiovascular failure marker.

A

LDH6

41
Q

What are the clinical significances of LDH?

A
  1. Myocardial Infarction: Elevates at 12-24 hours after onset, peaks at 48-72 hours, remains elevated for 10 days. 2. Hepatitis.
  2. Hemolysis.
  3. Lung and muscle disorders.
42
Q

methods for LDH measurement?

A
  1. Wacker method - Forward or direct, pH: 8.8, Absorbance: 340nm.
  2. Wroblewski Laude - Reverse or Indirect, pH: 7.2, Absorbance: 340nm.
43
Q

clinical significance of Myoglobin?

A

Marker of AMI: Elevates 2-3 hours after onset,
peaks at 8-12 hours,
normalizes 18-30 hours.

44
Q

clinical significance of Troponin I?

A

Elevates in AMI, elevates 3-6 hours after onset,
peaks at 12-18 hours after onset,
normalizes in 6 days.

45
Q

function of amylase

A

For the breakdown of glycogen and starch.

46
Q

What are the clinical significances of amylase?

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.
47
Q

methods for amylase measurement?

A
  1. Saccharogenic - measures reducing sugar from starch breakdown.
  2. Amyloclastic - also known as Iodometric method.
  3. Chromogenic - uses dye to check amylase activity.
  4. Coupled enzyme.
48
Q

measures reducing sugar from starch breakdown.

A

Saccharogenic

49
Q

known as Iodometric method.

A

Amyloclastic

50
Q

uses dye to check amylase activity.

A

Chromogenic

51
Q

Hydrolyze glycerol esters of long-chain fatty acids.

A

lipase

52
Q

In case of emergency, which is better usage for Acute Myocardial Infarction— CK MB or LDH?

A

CK MB, since after 4 hours you can detect the cause of chest pain is AMI. LDH is after 12 hours. However, for late diagnosis, LDH is better since it is still present within 10 days.

53
Q

In case of emergency, which is better usage for Acute Myocardial Infarction— Myoglobin or CK MB?

A

Myoglobin, since it is elevated after 2-3 hours. Issue in myoglobin is specificity due to many sources when it comes to muscle, but good in sensitivity.

54
Q

functions in the breakdown of triglycerides, which are a type of fat.

A

Lipase

55
Q

What are the clinical significances of lipase?

A

the clinical significances of lipase include acute pancreatitis, perforated or duodenal ulcer, intestinal obstruction, and mesenteric vascular obstruction.

56
Q

not commonly used for diagnosis due to specificity issues

A

LDH

57
Q

A heart failure biomarker. Derived from a prohormone.

A
  1. Brain-type natriuretic peptide
58
Q

Acinar cells of the pancreas

A

releases Amylopsin

59
Q

releases Ptyalin

A

Salivary glands

60
Q

Measure amylase activity by following decrease in substrate concentration

A

Amyloclastic

61
Q

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

A

LIPASE

62
Q

lipase synonym

A

TRIACYLGLYCEROL ACYLHYDROLASE

63
Q

o Transport and stores oxygen to intercellular respiratory enzymes of contractile cells (with high affinity to O2)

A

myoglobin

64
Q

o Found in myocardium and with greater cardiac specificity

A

troponin I

65
Q

Utilizes Olive oil for hydrolysis

A

Cherry Crandal

66
Q

Indicator of Cherry Crandal

A

Phenolphthalein

67
Q

reference method for Lipase

A

Cherry Crandal

68
Q

lactate dehydrogenase synonym

A

“L-lactate: NAD oxidoreductase”

69
Q

CREATINE KINASE synonym

A

“ATP-Creatine-N-Phosphotransferase”

70
Q

amylase synonym

A

“Alpha 1-4 Glucan 4 Glucohydrolase”

71
Q

o Function: Hydrolyze glycerol esters of long-chain fatty acids

A

Lipase