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Botany > CC LEC 2 - Enzymes > Flashcards

CC LEC 2 - Enzymes Flashcards

1
Q

most enzymes react at pH __but some are active in wider pH ranges

A

7.0- 8.0,

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2
Q

ALP –

pH

A

pH 9.0-10.0

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3
Q

Gastric enzyme – pH

A

pH 6.0

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4
Q

For each ?°C increase in temp. reaction rate doubles

until the protein is denatured

A

10

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5
Q

– should always be provided in excess so that the extent of the reaction does not depend on its concentration

A

Cofactors

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6
Q

What are measured in measurement of enz activity? (4)

A

INC in product
DEC in substrate
DEC in coenzyme
INC in altered coENZ

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7
Q

In coupled ENZ assay,

-what catalyzes its reaction, product formed becomes a substrate of intermediate reaction.

A

enzyme under analysis

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8
Q

In coupled ENZ assay,

-what produces an intermediate product that will be the substrate for the final reaction

A

Intermediate auxiliary enzyme

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9
Q

What absorbs light at 340 nm while NAD does not)

A

NADH

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10
Q

Usually involves the conversion of NAD to NADH or vice versa [what enzyme type in coupled ENZ)

A

indicator enzyme

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11
Q

catalyzes the final reaction

A

indicator enzyme

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12
Q

method for couple ENZ assay

measures single absorbance at fixed time, reaction is assumed to be linear over fixed time

A

fixed time

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13
Q

method for couple ENZ assay

multiple absorbances are measured

A

Continuous monitoring/kinetic assay

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14
Q

method for couple ENZ assay

more accurate because any deviation from linearity is readily observed

A

Continuous monitoring/kinetic assay

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15
Q

*most common cause of deviation from linearity

A

occurs when the enzyme is so elevated that all substrate is used early in the reaction time

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16
Q

Units to report enzyme levels when enzymes are quantified relative to
their activity rather than a direct measurement of concentration

A

Activity Units

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17
Q

amount of enzyme that will catalyze the reaction of 1umol of substance per minute under specified conditions

A

IU

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18
Q

Enzyme activity SI unit –

A

katal (mol/s)

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19
Q

How many nkat is in 1.0IU?

A

1.0 IU = 17nkat

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20
Q

When will enz act as REAGENTS

A

measure non enzymatic constituents like glucose, cholesterol

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21
Q

Enzymes as __

Used for methods quantifying substrates for the corresponding enzyme

A

Reagent

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22
Q

– chemically bonded to adsorbents such as agarose

A

Immobilized Enzyme

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23
Q

Systematic name of CK

A

Creatine-N-phosphotransferase

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24
Q

MW of CK

A

82000 Daltons

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25
Q

ENZ assoc with ATP regeneration

A

CK

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26
Q

Creatine + ATP (catalyzed by CK) will yield

A

creatine phosphate + ADP

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27
Q

minor tissue sources of CK

A

bladder, placenta, GIT, thyroid, uterus, kidney, lung, prostate, spleen, liver, pancreas

28
Q

CK levels are elevated in (3)

A

MI
Rhabdomyolysis
Muscular dystrophy

29
Q

CK isoenz
– brain type, migrates fastest to the
anode

A

CK-BB

30
Q

CK isoenz

Cannot pass blood-brain barrier, undetectable in blood

A

CK-BB

31
Q

CK isoenz

Elevated in patients with various carcinomas; may be useful tumor associated marker

A

CK -BB

32
Q

– hybrid type, less than 6% of total CK

A

CK-MB

33
Q

CK-MB – hybrid type, less than ?% of total CK

A

6

34
Q

are more sensitive markers of MI; they are released earlier and persist longer

A

Troponin I and T

35
Q

CK Isoenz
Following myocardial infarction, levels rise within 4-8 hours, peak at 12-24 hours, and return to normal after 48-72 hours

A

CK-MB

36
Q

CK isoenz

– muscle type, most common, migrates slowest to the anode

A

CK-MM

37
Q

atypical ck
– migrates midway between CK-
MM and CK-MB

A

Macro-CK

38
Q

atypical ck

CK-MM complexed with IgG, or CK-MM complexed with lipoproteins

A

Macro-CK

39
Q

atypical ck

In serum, 0.8-1.6%

A

Macro-CK

40
Q

atypical ck

Age and sex related

A

Macro-CK

41
Q

atypical ck

– bound to exterior surface of the inner mitochondrial membranes of muscle, brain, and liver cells

A

Mitochondrial CK (CK-MI)

42
Q

enzyme released from hemolyzed RBCs and appearing as a band cathodal to CK-MM

A

adenylate kinase

43
Q

may cause falsely elevated CK or CK-MB value

A

adenylate kinase

44
Q

– more sensitive and precise than electrophoresis if done properly

A

Ion-exchange chromatography

45
Q

ref mtd of isoenz meas

A

EF

46
Q

– measure enzyme concentration rather than enzymatic activity,

A

Immunoassays (Radioimmunoassay, immunoinhibition)

47
Q

mtd of isoenz meas

can detect inactive forms of enzymes

A

Immunoassays (Radioimmunoassay, immunoinhibition)

48
Q

CK MEAS

Tanzer Gilvarg coupled with

A

PK-LD-NADH system

49
Q

CK MEAS

Tanzer Gilvarg pH

A

9.0

50
Q

CK meas

Oliver Rosalki coupled with

A

HK-G-6-NADP system

51
Q

CK meas

Oliver Rosalki pH

A

6.8

52
Q

Tanzer gilvarg

ADP + ____◄PK► pyruvate + ATP

A

phosphoenolpyruvate

53
Q

Tanzer gilvarg

ADP + phosphoenolpyruvate ◄PK► __ + ATP

A

pyruvate

54
Q

Tanzer gilvarg

Pyruvate + NADPH + H+ ◄LD► ____ + NAD+

A

Lactate

55
Q

CK meas

2 to 6 times faster than forward reaction

A

Oliver Rosalki

56
Q

Oliver Rosalki
Creatine phosphate + __◄CK► creatine
+___

A

Creatine phosphate + ADP ◄CK► creatine

+ATP

57
Q

Oliver Rosalki

ATP + __ ◄HK► ADP + ___

A

ATP + glucose ◄HK► ADP + G-6-P

58
Q

Oliver Rosalki

__ + NADH ◄G-6-PD►__ + NADPH

A

G-6-P + NADH ◄G-6-PD► 6- phosphogluconate + NADPH

59
Q

CK errors

___ mg/dL hemoglobin interferes

A

> 320

60
Q

Errors in CK meas

Instability of CK – rapid inactivation of enzyme due to oxidation of ___ group

A

sulfhydryl

61
Q

Errors in CK meas
Instability of CK
Can be partially reversed by adding

A

sulfhydryl compounds: N- acetylcysteine, mercaptoethanol, thioglycerol, dithiotreitol

62
Q

– inactivates CK

A

Light exposure

63
Q

Light exposure inactivates CK Activity can be restored if specimen is (2)

A

1) stored in the dark at 4°C/7 days

2) 20°C/month if the assay used a sulfhydryl activator

64
Q

higher muscle mass results in __ CK levels

A

higher

65
Q

RR of ck M

A

15-160 U/L

66
Q

RR of ck F

A

15-130 U/L

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