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1) The enzyme that catalyzes the change in location of the functional group from one position to another within a compound is called Isomerase/Mutase.
                                                                                              
(Mutase)
2) The enzyme having low affinity for the substrate will have low/high km.
                                                                                             
(High km)
3) The competitive inhibitors increase the Vmax/km but the Vmax/km remains constant.
                                        
(Increase km but the Vmax remains constant)
4) The non- competitive inhibitors decrease the Vmax/km but the Vmax/km remains constant.
                                         
(Decrease Vmax but the km remains constant)
5) The process of induction of an enzyme is a coarse/fine control for regulation of enzyme activity.
                                                                                             
(Coarse control)
6) Arsenate binds to SH group of the enzyme to inhibit its activity and this mode of inhibition is competitive/Non competitive.
                                                                                            
(Non competitive)
7) In normal health LDH-1/LDH-2 is in greater concentration in plasma.
                                                                                            
(LDH-2)
8) Transferases are the enzymes which catalyze the transfer of reducing equivalents/groups other than reducing equivalents.
                                                           
(Groups other than reducing equivalents)
9) The enzyme activity increases 2/4 fold with every ten degree rise of temperature
                                                                                             
(2 fold)
10) The reaction rate is zero/first order when the enzyme activity is directly proportional to substrate concentration
                                                                                             
(first-order)
11) The reaction rate is zero/first order when the enzyme activity is independent of substrate concentration
                                                                                             
(Zero order)
12) When the substrate concentration is equal to km the reaction velocity is equal to Vmax/Half Vmax.
                                                                                             
(Half Vmax)
13) Pepsin/Trypsin has an optimum p H of 2.0.
                                                                                             
(Pepsin)
14) Hexokinase/ Glucokinase is inducible
                                                                                             
(Glucokinase)
15) Hexokinase/ Glucokinase is inhibited by feed back inhibition
                                                                                            
(Hexokinase)
16) Alkaline Phosphatase/Acid phosphatase rises in malignancy of prostate gland.
                                                                                            
(Acid phosphatase)
17) LDH/SGOT rises in hemolytic anemias.
                                                                              
(LDH-Lactate dehydrogenase)
18) Methotrexate inhibits dihydrofolate reductase by competitive/Non competitive inhibition.
                                                                                        
(Competitive inhibition)
19) Streptokinase/tPA causes intravascular bleeding as a side effect.
                                                                                          
(Streptokinase)
20) All the Proteolytic/ Lipolytic enzymes are Zymases in nature.
                                                                                      
(Lipolytic enzymes)
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Choose the correct answer-

1) The enzyme that catalyzes the change in location of the functional group from one position to another within a compound is called Isomerase/Mutase.

2) The enzyme having low affinity for the substrate will have low/high km.

3) The competitive inhibitors increase the Vmax/km but the Vmax/km remains constant.

4) The non competitive inhibitors decrease the Vmax/km but the Vmax/km remains constant.

5) The process of induction of an enzyme is a coarse/fine control for regulation of enzyme activity.

6) Arsenate binds to SH group of the enzyme to inhibit its activity and this mode of inhibition is competitive/Noncompetitive.

7) In normal health LDH-1/LDH-2 is in greater concentration in plasma.

8) Transferases are the enzymes which catalyze the transfer of reducing equivalents/groups other than reducing equivalents.

9) The enzyme activity increases 2/4 fold with every ten degree rise of temperature.

10) The reaction rate is zero/first order when the enzyme activity is directly proportional to substrate concentration.

11) The reaction rate is zero/first order when the enzyme activity is independent of substrate concentration.

12) When the substrate concentration is equal to km the reaction velocity is equal to Vmax/Half Vmax.

13) Pepsin/Trypsin has an optimum p H of 2.0.

14) Hexokinase/ Glucokinase is inducible.

15) Hexokinase/ Glucokinase is inhibited by feed back inhibition.

16) Alkaline Phosphatase/Acid phosphatase rises in malignancy of prostate  gland.

17) LDH/SGOT rises in hemolytic anemias.

18) Methotrexate inhibits dihydrofolate reductase by competitive/Non competitive inhibition.

19) Streptokinase/tPA  causes intravascular bleeding as a side effect.

20) All the Proteolytic/ Lipolytic enzymes are zymases in nature.

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