Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Clinical Biochem > Serum Enzymes > Flashcards

Serum Enzymes Flashcards

1
Q

What is the reference range for ALP

A

30-130 U/L

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

What is the reference range for LD

A

100-225 U/L

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

What is the reference range for ALT

A

Female <40 U/L
Male < 60 U/L

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

What is the reference range for AST

A

Female <35 U/L
Male <45 U/L

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

What is the reference range for CK

A

Female <200
Male <250

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

What is the reference range for GGT

A

<80 U/L

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

What is the reference range for AMY

A

30-150 U/L

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

What is the reference range of LIP

A

0-60 U/L

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

What is activation energy

A

the amount of energy needed to raise all the molecules in 1 mol of a a compound at a certain temperature to the transitional state at the peak of the energy barrier, this corresponds to the formation of an activated enzyme-substrate complex

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

What is an isoenzyme

A

a group of enzymes that catalyze the same reaction but are encoded by different genes, each isoenzyme has a different molecular structure and varying physical, immunological and biochemical properties

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

What is a cofactor

A

non-protein molecules needed for enzyme activity

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

What is an activator

A

inorganic cofactor that when bound to an enzyme icreases the enzymes activity

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

What is a coenzyme

A

organic, low molecular weight substances which combines with an inactive protein

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

What is an apoenzyme

A

an inactive form of an enzyme that requires a coenzyme to be converted into an active holoenzyme

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

What is a prostetic group

A

a coenzyme bound to an apoenzyme

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

What is a holoenzyme

A

the active form of an apoenzyme formed by the combination of the apoenzyme with its coenzyme

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

What is denaturation

A

a change in the structure of a protein accompanied by a loss of activity

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

What are causes of denaturation

A

extreme pH, elevated temperature, changes in ionic strength and chemical modifiers

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

What are enzymes

A

proteins that function as catalysts by lowering the activation energy

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

What is the optimum pH for most physiological enzymes

A

7.0-8.0

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

What do buffers do

A

control the pH of enzyme reactions

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

What is the optimal temperature for physiological enzymes

A

37C

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

What does a 10C increase in temperature do to the reaction rate

A

doubles it

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

What is the rate of reaction dependant on in zero order kinetics

A

enzymes

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

What is the rate of reaction dependant on in first order kinetics

A

substrate

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

What is competitive inhibition

A

the inhibitor is a structural analog of the substrate and competes for the active site

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

How do you overcome competitive inhibiton

A

adding more substrate

28
Q

What type of inhibition is competitive inhibition

A

reversible

29
Q

What is non-competitive inhibition

A

an inhibitor binds tot he enzyme at an allosteric site causing conformational changes in the enzyme structure

30
Q

What is uncompetitive inhibition

A

the inhibitor binds to the enzyme-substrate complex preventing the creation of products

31
Q

How are enzymes measured

A

the concentration of an enzyme is directly proportional to the measurable catalytic activity of the enzyme

32
Q

What are fix time methods

A

the reaction is started, incubated for a specified time at a set temperature and then the reaction is stopped and the change in absorbance is measured

33
Q

What are continuous monitoring methods

A

the reaction is started and incubated at a set temperature for a set time, the change in absorbance is measured at multiple time points or continuously until the reaction is stopped

34
Q

Where is ALP found

A

intestine, liver, bone and placenta as well as the surface of RBCs

35
Q

What is the significance of ALP

A

clinically significant sources are osteoblasts and hepatocytes, increased in bone diseases and liver issues as well as in dialysis patients and cancer

36
Q

What are the activators of ALP

A

zinc and magnesium

37
Q

What are the inhibitors of ALP

A

phosphate and anticoagulants

38
Q

What are the limitations of ALP testing

A

measurement should occur within 4 hours, ALP increases at 4C and RT, hemolysis is an interference

39
Q

What is the tissue distribution of LD

A

throughout the body though concentrated into the heart, liver, skeletal muscles, RBC, platelets and lymph nodes

40
Q

What is the clinical significance of LD

A

increased in hemolytic and megaloblastic anemia as well as in liver disease and myocardial infarction

41
Q

What is the coenzyme of LD

A

NAD

42
Q

What are the limitations of LD testing

A

a serum sample is prefered and samples should be stored at RT, hemolysis is an interference

43
Q

What is the tissue distribution of ALT

A

liver and kidneys

44
Q

What is the clinical significance of ALT

A

increased in hepatic diseases

45
Q

What is the coenzyme of ALT

A

vitamin B6

46
Q

What are the limitations of ALT testing

A

should be measured on the same day as collection, only stable at -70C, hemolysis is an interference

47
Q

What is the tissue distribution of GGT

A

kidney, bile ducts of liver, pancreas and liver

48
Q

What is the clinical significance of GGT

A

indicator of hepatobiliary disease, elevated in alcohol related issues

49
Q

What is the activator for GGT

A

magnesium

50
Q

What are the inhibitors of GGT

A

citrate, oxalate, fluoride

51
Q

What are the limitations of GGT testing

A

serum and plasma are stable at 4C, ethanol warfarin phenobarbital and phenytoin can cause a false increase

52
Q

What is the tissue distribution of CK

A

skeletal muscle, heart, brain

53
Q

What is the clinical significance of CK

A

skeletal muscle diseases and heart disease

54
Q

What is the activator of CK

A

magnesium

55
Q

What is the coenzyme of CK

A

ATP

56
Q

What are inhibitors of CK

A

All coagulants except heparin, Maganese, calcium, zinc, copper and excess magnesium

57
Q

What are limitations of CK testing

A

samples are stable for upto 48 Hr at 4C, hemolysis will intefere

58
Q

What is the tissue distribution of amylase

A

salivary glands, pancreas, ovaries, fallopian tubes and lungs

59
Q

What is the clinical significance of amylase

A

increased in salivary gland inflammation, acute pancreatitis and other intra-abdomin disorders

60
Q

What is the activator for amylase

A

calcium

61
Q

What are the inhibitors for amylase

A

all anticoagulants except heparin

62
Q

What are the limitations of amylase testing

A

stable at RT, morphine and opiates elevate

63
Q

What is the tissue distribution of lipase

A

pancreas, stomach and small intestine

64
Q

What is the clinical significance of lipase

A

elevated in acute pancreatitis, gastic or duodenal ulcers and intestinal obstruction

65
Q

What is are the cofactors of lipase

A

colipase and bile salts

66
Q

What are the limitations of lipase testing

A

stable at RT for 1 week, hemolysis is an inhibitor

Clinical Biochem (15 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions