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Clinical Chemistry 2 > Chapter 13 - Enzymes > Flashcards

Chapter 13 - Enzymes Flashcards

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0
Q

these are rxn catalysts

A

enzymes

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1
Q

are all enzymes proteins?

A

yes

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2
Q

the greek word of enzyme means

A

in yeast

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3
Q

primary structure refers to

A

sequence of amino acids

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4
Q

secondary structure refers to

A

alpha helix

beta pleated sheets

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5
Q

tertiary structure is

A

folding/3D

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6
Q

kelan may quaternary ang protein?

A

> 1 polypeptid

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7
Q

substance acted upon

A

substrate

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8
Q

found in enzyme; where substrate reacts

A

active site

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9
Q

found in enzyme; for regulation, inhibition etc

A

allosteric site

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10
Q

same function with the enzyme but in different form

A

isoenzyme

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11
Q

how are isoenzymes differentiated

A

electrophersis
solubility
heat stability
chemical inhibition

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12
Q

isoenzymes are different in ______ structure and same in _______ structure

A

primary; tertiary

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13
Q

non-CHON necessary for enzymatic activity

A

cofactors

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14
Q

type of cofactors

A

coenzyme

activator

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15
Q

organic type of cofactors

A

coenzyme

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16
Q

inorganic type of cofactors

A

activators

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17
Q

examples of activators

A 
Mg
Ca
Cl
Cu
Co
Fe
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18
Q

examples of coenzymes

A 
biotin
NAD
thiamine
pyrophosphate 
lipoic acid
flavin
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19
Q

coenzyme bound tightly to enzyme

A

prosthetic group

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20
Q

enzyme portionbound to prosthetic group

A

apoenzyme

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21
Q

prosthetic group + apoenzyme

A

holoenzyme

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22
Q

inactive form of an enzyme

A

proenzyme

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23
Q

classification of enzymes

A 
oxidoreductase
transferases
hydrolases
lyases
isomerases
ligases
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24
Q

what is the first digit in a pn enzyme’s code

A

classification of enzyme

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25
Q

what is the second digit in an enzyme’s code

A

subclass

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26
Q

responsible for the nomenclature of enzymes

A

IUB-EC

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27
Q

standard name of enzymes can be

A

substrate + “ase”

reaction + “ase”

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28
Q

enzyme responsible for oxidation reduction

A

oxidoreductase

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29
Q

enzyme responsible for the transfer of shit i don’t know what shit

A

transferase

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30
Q

enzyme responsible for hydrolysis

A

di ko alam eh

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31
Q

enzyme responsible for the removal of a group without hydrolysis

A

lyases

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32
Q

enzyme responsible for the interconversion of geometric npositional optical isomers

A

isomerase

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33
Q

enzyme responsible for the joining of two substrates

A

ligases

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34
Q

only example of a ligase

A

glutathione synthetase

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35
Q

two ways to allow product formation

A

giving more energy

using enzymes

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36
Q

energy required to raise all molecules in 1 mole of a compound at a certain temp to the transition state of the peak of energy

A

activation energy

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37
Q

types of specificity

A

absolute
group
bond
stereoisometric

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38
Q

optimum pH for most enzymes

A

7.0-8.0

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39
Q

optimum temp for most enzymes

A

37 oC

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40
Q

at what pH does trypsin work

A

1.0

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41
Q

high temp ________ enzymes

A

denatures

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42
Q

low temp ________ enzymes

A

inactivates

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43
Q

for every _____ increase in temp, rxn is doubled

A

10 oC

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44
Q

this shows the relationship betweenvelocity and substrate conc

A

Michaelis-Menten constant

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45
Q

the maximum point in the Michaelis-Menten curve is also the

A

saturation point

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46
Q

the point kung saan no matter gaano kadaming enzyme ang ilagay there is no more reaksyon na mangyayari

A

saturation point

jk di kosure kung ganyan ba un

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47
Q

types of inhibition

A

competitive
noncompetitive
uncompetitive

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48
Q

inhibitor binds direly to active site, reversible

A

competitive

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49
Q

inhibitor binds to a site other than thrpe active site

A

noncompetitive

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50
Q

when is noncompetitive inhibition irresversible

A

if damage is brought to the catalytic site

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51
Q

inhibitor binds to ES complex itself

A

uncompetitive

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52
Q

increased substrate in uncompetitive inhibition would _____ inhibition

A

worsen

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53
Q

the enzyme combines with only one substrate

A

absolute specificity

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54
Q

enzyme combines with all substrates contain a particular chemical group

A

group specific

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55
Q

enzymes combines to substrates with certain chemical bonds

A

bond specificity

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56
Q

enzymes that predominantly combine with only one optical isomer of a certain compound

A

stereoisometric specificity

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57
Q

the rxn rate is directly proportional to substrate conc.

A

first order kinetics

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58
Q

how is enzyme activity measured? thru:

A

increase in product formation
decrease in substrate formation(conc ata hindi form)
decrease in coenzyme formation
increase in conc of altered shitshit

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59
Q

amount of enzyme that will catalyze the rxn if 1 micromole of substrate per minute under specified condition enzyme activity

A

IU (kung anuman un)

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60
Q

two methods of enzyme activity measurement

A

fixed time/endpoint

continuous monitoring/kinetic assay

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61
Q

how many times is absorbance read in fixed time/endpoint

A

once

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62
Q

what are the major enzymes

A

TMTM

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63
Q

minor enzymes

A 
OCT
POD
GOD
ALS
LAP
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64
Q

the recommended (?) name of creatine kinase

A

ATP:creatine-N-phosphotransferase

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65
Q

size of CK

A

82000 da

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66
Q

CK is associated mainly with _______ generation

A

ATP

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67
Q

major tissue sources of CK

A

skel muscle
heart
brain

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68
Q

minor tissue sources of CK

LLPPS PG BTUK

A 
lung 
liver 
pancreas 
prostate 
spleen
placenta
GIT
bladder
thyroid
uterus
kidney
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69
Q

isoenzyme of CK

A

CK-MB
CK-MM
CK-BB

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70
Q

which CK isoenzyme is fastest toward anode

A

CK-BB

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71
Q

most electronegative CK isoenzyme

A

CK-BB

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72
Q

isoenzyme rarely seen in serum, mainly found in brain

A

CK-BB

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73
Q

least concentration among the CK isoenzymes

A

CK-BB

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74
Q

which CK isoenzyme is a hybrid

A

CK-MB

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75
Q

CK isoenzyme found mainly in the heart

A

CK-MB

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76
Q

CK isoenzyme found mainly in the skeletal muscle

A

CK-MM

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77
Q

normal CK-MB conc in total CK

A

<6%

78
Q

two atypical isoenzyme of CK

A

mitochondrial CK

macro CK

79
Q

where does mitochondrial CK migrate

A

before CK-MM (before origin)

80
Q

CK isoenzyme indicating severe illness

A

mitochondrial CK

81
Q

CK detected in cases of malignant tumor and cardiac abnormality

A

mitochondrial CK

82
Q

where does ,acro CK migrate to

A

between MM and MB

83
Q

this isoenzyme is CK-MM complexed with IgG, some IgA or lipoprotein

A

macro CK

84
Q

age-sex related isoenzyme of CK

A

macro CK

85
Q

normal conc. of macro CK

A

.8-1.6%

86
Q

methods of CK isoenzyme measurement

A

electrophoresis
ion exchange chromatography
immunoassays
double antibody inhibition

87
Q

what is visualized in electrophoresis of CK that is cathodal to CK-MM

A

AK (kung ano man yan)

88
Q

immunoassay of CK isoenzymes use antibodies against ____________

A

H and B subunit

89
Q

methods of CK det

A

Tanzer-Gilvarg

Oliver Rosalki

90
Q

optimum pH of Tanzer Gilvarg

A

9.0

91
Q

CK det method coupled w/ PK-LD-NADH system

A

Tanzer Gilvarg

92
Q

forward type of CK det method

A

Tanzer Gilvarg

93
Q

optimum pH of Oliver Rosalki

A

6.8

94
Q

Ck det method coupled w/ HK-G6PD-NADP system

A

Oliver Rosalki

95
Q

which is faster? Tanzer Gilvarg or Oliver Rosalki?

A

Oliver Rosalki

96
Q

ref range of CK in males

A

15-160 U/L

97
Q

CK-MB conc of >6% indicates

A

myocardial infarction

98
Q

ref range of CK in females

A

15-130 U/L

99
Q

instability of CK is resolved with

A

sulfhydryl compounds

100
Q

example of sulfhydryl compounds

A

dithiothreitol

thioglycerol

101
Q

does light inactivate CK

A

yes

102
Q

higher CK values in men are attributed to incresed

A

muscle mass

103
Q

enzyme responsible for interconversion of lactic and pyruvic acid

A

lactate dehydrogenase

104
Q

how does LD work

A

transfer H+ using coenzyme NAD+

105
Q

major tissue source of LD

A

heart
liver
skel muscle
erythrocytes

106
Q

minor tissue sources of LD

A

lung

smooth muscle

107
Q

diagnostic significance of LD

A 
cardiac
hepatic
skel disease
renal
pernicious anemia
108
Q

isoenzymes of LD

A

LD1 - LD6

109
Q

fastest LD isoenzyme

A

LD1

110
Q

highest conc among LD isoenzyme

A

LD2

111
Q

highest affinity to anode LD isoenzyme

A

LD1

112
Q

an LD idornzyme that is a bad prognosis and indicates impending death

A

LD6

113
Q

order of LD isoenzymes most con to lowest conc

A

2 > 3 > 1 > 4 > 5

114
Q

an atypical LD isoenzyme

A

macro LD

115
Q

found between LD3 and LD4

A

macro LD

116
Q

LD1 conc higher than LD2 indicates

A

myocardial infection

117
Q

highest affinity LD isoenzyme to anode

A

LD1

118
Q

methods for LD measurement

A

Wacker

Wroblewski La Due

119
Q

endpoint of Wacker method

A

blue purple color

120
Q

mol weight of LD

A

128000 da

121
Q

LD6 is called

A

alcohol dehydrogenase

122
Q

which LD measurement methd is forward

A

Wacker

123
Q

by how many tomes is Wroblewski La Due faster than Wacker

A

3x

124
Q

other name for AST

A

serum glutamic oxaloacetatic transaminase

125
Q

major tissue sources of AST

A

cardiac muscle
skel muscle
liver

126
Q

minor tissue sources of AST

A

kidney
pancreas
RBCs

127
Q

methods for AST det

A

Reitman-Frankel

coupling with diazonium salts

128
Q

mechanism of Reitman-Feankel

A

ketoacids is reacted to 2,4-dinitrophenylhydrazine (DNPH)

129
Q

product of Reitman-Frankel

A

ketoacid hydrazones

130
Q

falsely decreases AST level

A

mercury
cyanide
fluoride

131
Q

example of liver diseases

A

viral hepatitis

cirrhosis

132
Q

is AST useful in diagnosis of AMI

A

hindi eh

133
Q

example of skeletal muscle disorder

A

muscular dystrophies

134
Q

the optimum pH for Karmen method

A

7.3-7.8

135
Q

absorbance of AST Karmen method

A

340nm

136
Q

AST activity is stable in serum for ______ days at ref temp

A

3-4 days

137
Q

catalyzes transfer of an amino group from alanine to alpha ketoglutarate wih the formation of glutamate and pyruvate

A

alanine aminotransferase

138
Q

old term for ALT

A

serum glutamic pyruvic transaminase

139
Q

major tissue source of ALT

A

liver

cardiac tissue

140
Q

diagnostic significance of ALT

A

hepatic parenchymal disease
AMI or heart failure
IM
muscular dystrophy

141
Q

most labile LD isoenzyme

A

LD5

142
Q

LD activity in serum is _______

A

unstable

143
Q

how is sample for LD stored

A

25 oC

144
Q

gaano katagal dapat matest ang LD

A

within 48hrs

145
Q

gaano katagal dapat matest ang LD isoenzyme

A

24hrs

146
Q

ref range of LD

A

125-220 U/L

147
Q

half life of ALT

A

24hrs

148
Q

indicator enzyme for ALT assay

A

LD

149
Q

absorbance for ALT

A

340nm

150
Q

methods for ALT measurement

A

Karmen
Reitman
coupling w/ diazonium salt

151
Q

unaffected by hemolysis

A

ALT

152
Q

stability of ALT

A

3-4days at 4 oC

153
Q

ref range for ALT

A

6-37 U/L

154
Q

catalyzes hydrolysis of various phosphomonoesters at an alkaline pH

A

alkaline phosphatase

155
Q

coenzyme for ALP

A

pyridoxal phosphate

156
Q

activator for ALP

A

Mn

Mg

157
Q

optimal pH for ALP

A

9.0-10.0

158
Q

major tissue source of ALP

A 
intestine
liver
bone
spleen 
placenta 
kidney
159
Q

ALP isoenzymes

A

liver ALP
bone ALP
placenta ALP
intestinal ALP

160
Q

diagnostic significance of ALP

A

hepatobiliary

bone disorders

161
Q

in bone disorders, there is elevation in ALP when ____ are involved

A

osteoblast

162
Q

example of bone disorder where ALP is elevated

A

Paget’s disease

163
Q

which ALP isoenzyme migrates the fastest

A

liver ALP

164
Q

liver is further divided into

A

major liver band

fast or alpha 1

165
Q

who are most likely to possess intestine ALP

A

blood type B and O

secretors

166
Q

ALP isoenzyme differentiation

A

electrophoresis
heat stability
chemical inhibition

167
Q

order of ALP isoenzymes in electrophoresis

A

fast > major > Regan Nagao > bone > placenta > intestinal

168
Q

which ALP isoenzyme resust denaturation at 65 oC for 30 minutes

A

placental ALP

169
Q

atypical ALP isoenzyme

A

Regan Nagao

170
Q

other name for Regan Nagao

A

carcinoplacental ALP

171
Q

ectopic product of an enzyme by malignant tissue

A

Regan isoenzyme

172
Q

may be considered a variant of Regan isoenzyme

A

Nagao

173
Q

what inhibits Nagao

A

L-leucine

174
Q

which best inhibits intestinal and placentaL ALP

A

phenylalanine

175
Q

detected in metastatic carcinoma and adenocarcinoma

A

Nagao

176
Q

mechanism of Bowers McComb (ALP)

A

p-nitrophenylphosphate -> p-nitrophenol + phosphate ion

177
Q

absorbance sa Bowers McComb

A

405nm

178
Q

high fat meals _______ ALP

A

increase by 25%

179
Q

ref range of ALP

A

30-90 U/L

180
Q

optimal pH for ACP

A

5.0

181
Q

tests for ALP

A 
Bodansky
King-Armstrong or Cutman Gutman
Bessey-Lowry-Brock 
Hudson
Babson Reed 
Bowers McComb
Sinowara Jones Reinhart
182
Q

basic difference in ALP and ACP

A

pH

183
Q

major tissue source of ACP

A

prostate

184
Q

minor source of ACP

A 
bone
liver
spleen
kidney
erythrocytes
platelets
185
Q

diagnostic significance of ACP

A

hyperplasia of prostate
rape cases
bone disease
heart cancer

prostatic carcinoma
metastatic carcinoma

186
Q

most specific substrate for prostatic ACP

A

thymolphthalein monophosphate

187
Q

chemical inhibition of prostatic ACP usually uses ____ as inhibitor

A

tartrate

188
Q

formula for pACP

A

total ACP - ACP after tartrate inhibition

189
Q

PSA stands for

A

prostate-specific antibody

190
Q

inhibitor for non-pACP

A

copper

191
Q

serum activity _____ within _______ if the sample is left at rm tmp unpreserved

A

decrease; 1-2hrs

192
Q

ref range for ACP

A

0-35 ng/mL

193
Q

upon clotting, serum for ACP det must be

A

separated immediately

Clinical Chemistry 2 (11 decks)

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