Acetazolamide is a drug which inhibits carbonic anhydrase. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. Figure 2 shows the experimental curve of initial reaction velocity (as percentage of V) versus [S] (concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the presence of acetazolamide. 100 No inhibitor Acetazolamide 0.2 0.4 0.6 0.8 (8) (mM) Figure 2 (i) Compare the maximal velocities and Michaelis Menten constants of the enzyme in the absence and the presence of the inhibitor acetazolamide. Determine the nature of inhibition by acetazolamide. Explain your answer. AJO %)A

Curren'S Math For Meds: Dosages & Sol
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Chapter9: Parenteral Medication Labels And Dosage Calculation
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Problem 7.7P
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Acetazolamide is a drug which inhibits carbonic anhydrase. Carbonic anhydrase participates
in regulation of the pH and bicarbonate content of a number of body fluids. Figure 2 shows
the experimental curve of initial reaction velocity (as percentage of Vma) versus [S]
(concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the
presence of acetazolamide.
100
No inhibitor
50
Acetazolamide
0.2
0.4
0.6
0.8
[S] (mM)
Figure 2
(i)
Compare the maximal velocities and Michaelis Menten constants of the enzyme in
the absence and the presence of the inhibitor acetazolamide. Determine the nature of
inhibition by acetazolamide. Explain your answer.
(ii)
Name TWO (2) other types of inhibitions besides the inhibition shown by
acetazolamide. Sketch a graph of V versus [S] showing curves in the absence of an
inhibitor and in the presence of the types of inhibitors not shown by acetazolamide.
("AJO %) A
Transcribed Image Text:Acetazolamide is a drug which inhibits carbonic anhydrase. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. Figure 2 shows the experimental curve of initial reaction velocity (as percentage of Vma) versus [S] (concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the presence of acetazolamide. 100 No inhibitor 50 Acetazolamide 0.2 0.4 0.6 0.8 [S] (mM) Figure 2 (i) Compare the maximal velocities and Michaelis Menten constants of the enzyme in the absence and the presence of the inhibitor acetazolamide. Determine the nature of inhibition by acetazolamide. Explain your answer. (ii) Name TWO (2) other types of inhibitions besides the inhibition shown by acetazolamide. Sketch a graph of V versus [S] showing curves in the absence of an inhibitor and in the presence of the types of inhibitors not shown by acetazolamide. ("AJO %) A
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