The kinetics of inhibition by acetazolamide and sulfanilamide of the formation of carbon dioxide from bicarbonate, catalyzed by partially purified carbonic an-hydrase preparations from bovine erythrocytes, were those of competitive inhibition. This is contrasted with the non-competitive kinetics of sulfonamide inhibition of a number of carbonic anhydrase-mediated hydration reactions. K1 for acetazolamide was 8.6 × 10-8 M while that for sulfanilamide was 1.8 × 10-5 M; these values are similar to those reported for inhibition of CO2 hydration in the presence of bovine erythrocyte enzyme.
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Leibman et al. (1967) studied this question.