LESSON 2 (part2) Flashcards
This talks about the hydrogen Ion concentration
pH
This talks about the point which the concentration rate is greatest.
Optimum pH
At what pH does many enzymes shows maximum activity?
7.0 - 8.0
At what pH is Pepsin active?
1.5
At what pH is ALP active?
10.5
This binds the substrate to the active site by forming ionic bridges and orients the substrate so it is attached to the enzyme in the correct configuration.
Activators
What is the common activator?
Magnesium
This decreases the rate of enzyme reaction and counterpart of activators.
Inhibitors
Describe the ff:
A. Competitive Inhibition
B. Non-competitive Inhibition
C. Uncompetitive Inhibition
A. Competes with the substrate
B. Freely attached and will not compete to the substrate.
C. The inhibitor will bind to the E-S complex
Enumerate the type of Inhibition
A. Reversible INhibition
B. Irreversible Inhibition
Describe the following:
A. Reversible INhibition
B. Irreversible Inhibition
a. Inhibitors are possibly removed from the system. Therefore, the enzyme is fully restored.
B. Inhibitors covalently combined with the enzyme
What are the examples f iNhibitors?
- Excess substrate
- Product of Inhibition
- E-S complex does not break to yield products
- Chemical substances
This inhibitor causes COMPETITION between substrate and molecules for a single binding site.
Excess substrate
This maybe an inhibitor of the forward reaction.
Product of reaction
This is the loss of enzymatic activity.
Enzyme denaturation
Enumerate the reasons for Enzyme Denaturation.
- Disruption of the 3-dimensional structure of the enzyme molecule.
- May be reversed if: denaturation is not extensive OR denaturing agent is removed
- Elevated temperature - beyond 50 - 60’C
- Extreme in pH
- Radiation
- Frothing
- Strong salt solution
- Mechanical trauma
- Chemicals
MEASUREMENT OF ENZYME REACTION:
The rate of an enzyme - catalyzed reaction is ___________________ to the amount of ________________ present in the system.
Directly proportional; active enzyme
What are the methods of Enzyme Assay?
- Fixed Time Assays
- Continuous-MOnitoring or KINETIC ASSAYS
This Assay uses a serum+substrate where the reactants are combined and the reaction proceeds for a designated time and is stopped by inactivating the enzyme.
Fixed Time Assays
This Assay has multiple measurements made at specific time intervals or by a continuous recording spectrophotometer.
Continuous-Monitoring or Kinetic Assays
What are the Units of Measurement of enzymes?
IU and Katal
This unit of measurement is proposed by the Commission on Enzymes (IUB) and is expressed in terms of U/L or mU/L
IU
This unit of measurement is the unit of enzyme activity w/c converts 1 mol of substrate per second. Conforms with the System International (SI) scheme of units.
Katal
Enumerate the sources of errors in enzyme Assay.
- Use of plasma
- Hemolysis
- Turbid/Lactascent Serum
- Heat Labile enzyme
- Contaminants
In performing enzyme assays this specimen is the least preferred.
The use of plasma
This is the inhibitory effects of anticoagulant on enzyme activity.
Use of Plasma
This happens upon the release of intercellular enzyme.
Hemolysis
This inhibits CK and Amylase
Turbid/ Lactascent Serum
What are the factors that influence the rate of entry?
A. Leakage of enzymes from cells
B. Altered enzyme production
This type of factor that influences the rate of entry talks about the impaired energy production: promote deterioration of cell membrane and directly attacks on the cell membranes.
Leakage or Enzymes from Cells
What causes the decrease of altered enzyme production?
genetic deficiency of enzyme production and;
the enzyme production is depressed as a result of diseases.
GIve example of Altered enzyme production.
Mucopolysaccharidoses
This is the accumulation of sugar complexes.
Mucopolysaccharidoses
What is the cause of the increase of Altered Enzyme Production?
Increase in the # and activity of cells
Enzyme Induction
Proliferation of enzyme-producing cells
This is the effect of drugs and other substances
Enzyme Induction
