Effect of Chlorthalidone Binding on the Electrophoretic Properties of Human Red Cell Carbonic Anhydrase Isozymes
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The manner in which aromatic sulfonamide inhibitors bind to the carbonic anhydrases can provide us with useful information concerning the mechanisms of carbonic anhydrase action. Although considerable data are now available on carbonic anhydrase-sulfonamide binding kinetics (cf. Maren, 1967; Lindskog et al,, 1972), much less is known about structural changes in carbonic anhydrase brought about by sulfonamide binding. Recently, spectral analyses by King and Burgen (1970) and King and Roberts (1971) of sulfonamide complexes with human carbonic anhydrases, indicate that conformational changes occur in the enzymes as a result of the sulfonamide binding. In the present brief communication, we report some preliminary findings which may provide additional evidence for sulfonamide-induced conformational changes in carbonic anhydrase molecules.
KeywordsCarbonic Anhydrase Esterase Activity Electrophoretic Pattern Carbonic Anhydrase Action Human Carbonic Anhydrases
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