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