1 |
A little change in phmay leadsto. |
- A. Effects enzyme only in high concentration
- B. Retarder even block enzyme activity
- C. Ionization of substrate
- D. Ionization of active sites of enzyme
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2 |
The rate of an enzyme catalyzed reaction |
- A. Is constant under condition
- B. Decreases as substrate concentration increases
- C. Cannot be measured
- D. Can be reduced by inhibitors
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3 |
Co-enzyme is a |
- A. Covalently bonded non-protein part of an enzyme
- B. Loosely bonded non-protein part of an enzyme
- C. Co-factor consists of metal ions
- D. None of these
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4 |
An enzyme is said to be denatured when |
- A. It has no co-factor
- B. It is in a condition of low temperature
- C. Its structure is destroyed
- D. None of these
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5 |
An activated enzyme consisting of a polypodies chain and a co factor is called. |
- A. Apo enzyme
- B. Co enzymes
- C. Holo enzymes
- D. Both a and b
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6 |
Optimum pH values for enzyme arginase is |
- A. 7.60
- B. 9.70
- C. 8.60
- D. 9.52
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7 |
If more substrate to an already occurring enzymatic reaction is added more enzyme activity is seen because |
- A. There is probably more substrate present than there is enzyme
- B. There is probably more enzyme available than there is substrate
- C. There is probably more product present than either substrate or enzyme
- D. The enzyme substrate complex is probably failing to from during the reaction
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8 |
Metals is ions are related to. |
- A. Co enzymes
- B. Vitamins
- C. Co factors
- D. Substrate
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9 |
The active site of an enzyme |
- A. Never changes
- B. Forms no chemical bond with substrate
- C. Determines by its structure the specificity of an enzyme
- D. Looks like a lump projection from the surface of an enzyme
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10 |
The optimum pH of salivary amylase is. |
- A. 2.80
- B. 4.80
- C. 6.80
- D. 8.80
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