問題一覧
1
an active substance formed by combination of a co enzyme and an apoenzyme
holoenzyme
2
??
Alanine aminotransferase
3
substance added in the enzyme substrate complex to manifest the enzyme activity
cofactors
4
Removal of groos from substrates without hydrolysis
lyases
5
??
L tartate ions
6
_ levels begin ti rise in _ peak at _ and return to norman in _ days.
AST, 6-8 hrs, 24hrs and 5 days
7
proteins that catalyze biochemical rxns
enzyme
8
Fight for active site
Competitive inhibitor
9
Reverse reaction (pyruvate to lactate
Wrobleuski- La due
10
muscle type; slowest; stiriated muscle and normal serum
CK-3/ CK MM
11
only a fixed number of substrate is converted to product per sec; even more product = no rxn
zero order kinetics
12
End point; once or twice
Fixed time (two poin) assay
13
??
Gamma glutamyl transferase
14
measurements at specific time intervals
continous monitoring (kinetic assay)
15
subject to denaturation in which enzyme looses its activity
apoenzyme
16
inhibits red cell acp
formaldehyde
17
Hybrid type; 2nd fastest and heart tissues
CK-2/ CK-MB
18
soecific for their particular enzyme
Substrates
19
an inactive enzyme precursor
proenzyme/ zymogens
20
Per minute in measuring enzymatic rxn
continous monitoring (kinetic assay)
21
Joins 2 substrate molecules, coupled with breaking of pyrophosphate bond in ATO
Ligases
22
A cavity other than the active site that binds regulatory molecules
allosteric site
23
uses malate dehydrogenase; measure ⬇️ in absorbancr at 340nm
Karmen method
24
Measure ⬇️ in abs. at 340nm
Forward reaction Tanzer givarg
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The ast/ ALT RATIO of >1
Non viral origin (alcohol)
26
combines with only 1 susbstrare and catalyzes only one rxn
absolute specificicity
27
??
Walker method
28
??
pancreatic amylase
29
??
Acid phosphatase
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Reaction rate is proportional to the substrate reaction; more substrate = more product
First order kinetics
31
similar enzymatic activity but differ in physical biochrmical and immunological characteristics
isoenzyme
32
interconversions of geomteric optical or positional isomers
isomerases
33
Highest activities in cardiac liver and skeletas muscle
Aspartare aminotransferase
34
catalyze the transfer of a group between 2 substrates
transferases
35
widely distributed, highest activities in heart, liver skeletal muscle and RBC
LDH
36
forward reaction (lactate to pyruvate)
Wrobleuski- cabaud or wacker method
37
second columnn
ALT / SGPT
38
??
Liver alp
39
A cavity of an enzyme where substrates bind and undergo a chemical reaction
Active site
40
??
Alkaine phosphatase
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combine with one optical isomer
sterioisometric specificity
42
combine with all substrates containing a particular chem group
group specificity
43
???
szaz assay
44
Total Ck dtermination of M:
15-160 u/l
45
the protein portion of the enzyme
apoenzyme
46
First columnn
AST/ SGOT
47
??
intestinal alp
48
⬆️ in hepatocellular and skeletas muscle
Aspartate aminotransferase
49
Found in body tissye and is increased un serum after cell injury
Enzyme
50
?
bone alp
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catalyzes hydrolysis of various bonds
hydrolases
52
??
Bowers and Mccomb
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Total LDH determination includes that LD begin to rise within _ peak at_ and remains eleveated for _ days.
10-24hrs, 48-72 hrs and 10 days
54
the ast/ alt ratio that is <1
viral in origin
55
calculation of enzyme activity includes
IU (EC)umol/mins, KAT(SI) mol/s
56
with substrate but still didikit padin; kabet
Uncompetetive inhib
57
specific to chemical bonds
bond specificity
58
in pregnancy alp
placental alp
59
??
amylase
60
fight for Allosteric site; once na naka locate na don wala ng ddikit
non competetive inhibitor
61
total ck determination for ck-mb
<6% of total CK
62
Measure ⬆️ in abs. at 340nm
Reverse reaction
63
??
salivary amylase
64
Brain type; Fastest and CNS GIT & uterus (preggy)
CK-1/ CK-BB
65
??
Lipase
66
Rgts are combines and the amt of rxn is measured
Fixed time (two point assay)