1S [LAB]: AST & ALT Flashcards
Biologic proteins that catalyze chemical reaction without altering the equilibrium point of the reaction without being consumed or changed in composition
Enzyme
Enzymes are found in all body tissue, frequently appearing in ___ following cellular injury or from degraded cells
Serum
The part of the enzyme where the substrate binds
Active site
The part of the enzyme where the catalytic action happens
Active site
Substance acted upon in an enzymatic reaction
Substrate
Water free cavity where the substrate interacts with particular charged amino acid residues
Active site
A cavity other than the active site which binds the regulator molecules
Allosteric site
Give the class of the enzyme based on the EC code:
1
Oxidoreductase
Give the class of the enzyme based on the EC code:
2
Transferase
Give the class of the enzyme based on the EC code:
3
Hydrolase
Give the class of the enzyme based on the EC code:
4
Lyase
Give the class of the enzyme based on the EC code:
5
Isomerase
Give the class of the enzyme based on the EC code:
6
Ligase
A/n ___ increase in temperature doubles enzymatic activity
10C
Too high temperature causes the enzyme to ___
denature
Non-protein molecule of enzymes necessary for enzyme activity
Cofactors
Inorganic cofactors are also known as ___
Activators
Organic cofactors are also known as ___
Coenzymes
Tell whether the given is an activator or a coenzyme:
Chloride
Activator
Tell whether the given is an activator or a coenzyme:
Bromide
Activator
Tell whether the given is an activator or a coenzyme:
Magnesium
Activator
Tell whether the given is an activator or a coenzyme:
Iron
Activator
Tell whether the given is an activator or a coenzyme:
Zinc copper
Activator
Tell whether the given is an activator or a coenzyme:
Calcium
Activator
Tell whether the given is an activator or a coenzyme:
Manganese
Activator
Tell whether the given is an activator or a coenzyme:
Cobalt
Activator
Tell whether the given is an activator or a coenzyme:
Potassium
Activator
Tell whether the given is an activator or a coenzyme:
Thiamine
Coenzyme
Tell whether the given is an activator or a coenzyme:
Pyrophosphate
Coenzyme
Tell whether the given is an activator or a coenzyme:
Cobamide
Coenzyme
Tell whether the given is an activator or a coenzyme:
Biotin
Coenzyme
Tell whether the given is an activator or a coenzyme:
Nicotinamde
Coenzyme
Tell whether the given is an activator or a coenzyme:
Pyridoxal
Coenzyme
Tell whether the given is an activator or a coenzyme:
Phosphate
Coenzyme
Tell whether the given is an activator or a coenzyme:
Folic acid
Coenzyme
The measurement of enzyme activity is done at ___ order kinetics
Zero
Zero order kinetics means that the measurement is not dependent on the concentration but on its ___
Activity
The amount of enzyme that will catalyze the reaction of 1 umol of substrate per minute under specified condition
IU (international units)
The unit for enzyme activity is ___
katal (mol/s)
1.0 UI = ___ nkat
17
The old name for aspartate aminotransferase
Serum glutamic oxaloacetic transaminase/ transferase
Involved in the transfer of an amino group between aspartate and a-keto acids
Aspartate aminotransferase/ SGOT
The measurement of AST uses ___ as coenzyme
Pyridoxal phosphate
Tissue sources of AST include:
Cardiac tissue, liver, skeletal muscle, kidney, pancreas, erythrocytes
Tell whether the AST will be increased or decreased in the given conditions:
AMI
Increased
Tell whether the AST will be increased or decreased in the given conditions:
Congestive heart failure
Increased
Tell whether the AST will be increased or decreased in the given conditions:
Hepatocellular disorders
Increased
Tell whether the AST will be increased or decreased in the given conditions:
Skeletal muscle disorders
Increased
Tell whether the AST will be increased or decreased in the given conditions:
Pulmonary embolism
Increased
Tell whether the AST will be increased or decreased in the given conditions:
Acute pancreatitis
Increased
Tell whether the AST will be increased or decreased in the given conditions:
Uremia
Decreased
AST isoenzymes include:
Cell cytoplasm AST
Mitochondrial AST
This AST isoenzyme is increased in cellular necrosis
Mitochondrial AST
Most commonly used method in AST determination
Karmen method
Karmen method is done through the measurement of absorbance at ___nm
340 nm
Optimal pH for the Karmen method
7.3-7.8
In the first reaction in Karmen method, the AST reacts with L-aspartate and oxoglutarate to form ___ and ___
Oxaloacetate and L-glutamate
In the second reaction in Karmen method of AST determination, the ___ reacts with oxaloacetate and NADH to form ___ and NAD
Malate dehydrogenase
L-malate
An AST/ALT determination method where the ketoacids is reacted to 2,4-dinitrophenylhydrazine (DNPH) to form ketoacid hydrazones
Reitman-Frankel method
The product of Reitman-Frankel method
Intense brown color
When using the Reitman-Frankel method of AST/ALT determination, a wavelength of ___nm is used
505 nm
An AST/ALT determination method where ketoacid and diazo compound reacts to form diazonium derivative
Coupling with diazonium salts
In the Karmen method of AST determination, the indicator reaction is catalyzed by ___ and the change in absorbance is monitored as NADPH is ___ to NAD
Malate dehydrogenase
Oxidized
Old name for alanine aminotransferase
Serum glutamic pyruvic transaminase/ transferase
AST/ ALT:
Better measure for liver cirrhosis and cardiac marker
ALT
Catalyzes the transfer of an amino group from alanine to a-ketoglutarate
Alanine aminotransferase
In ALT measurement, ___ acts as coenzyme
Pyridoxal phosphate
Tissue sources of ALT
Liver, cardiac tissue
In the Karmen method of ALT determination, the indicator reaction is catalyzed by ___ and the change in absorbance is monitored as NADPH is ___ to NAD
Lactate dehydrogenase
Oxidized
In the first reaction of the Karmen method of ALT determination, L-alanine and oxoglutarate reacts with ALT to form L-glutamate and ___
Pyruvate
In the second reaction of the Karmen method of ALT determination, Pyruvate and NADH will react with ___ to form ___ and NAD
Lactate dehydrogenase
L-lactate
Determine whether the interference causes a false increase or false decrease:
Bilirubin
False increase
Determine whether the interference causes a false increase or false decrease:
Erythromycin
False increase
Determine whether the interference causes a false increase or false decrease:
Iproniazid
False increase
Determine whether the interference causes a false increase or false decrease:
Morphine
False increase
Determine whether the interference causes a false increase or false decrease:
Endogenous pyruvate
False increase
Determine whether the interference causes a false increase or false decrease:
Heavy metals like mercurial diuretics
False decrease
The ratio of reagent 1 to reagent 2 to form the working reagent
4:1
Determine whether the interference causes a false increase or false decrease:
Hemolysis
False increase
T/F: In ALT determination, hemolysis causes a dramatic increased effect on the result
False (It is relatively unaffected by hemolysis)
T/F: In ALT determination, hemolysis causes a dramatic increased effect on the result
False (It is relatively unaffected by hemolysis)
Optimal pH for enzymatic reactions
7.0-8.0