Inhibition of carbonic anhydrase by sulphonamides

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Abstract
The inhibitory action of 25 sulfonamides on carbonic anhydrase was examined at 0[degree] and 15[degree]C and in the presence and absence of a tissue homogenate. The most powerful inhibitors were prontosil red and prontosil soluble. Inhibition decreased with rise in temp., the temp. coefficient changing markedly with the sul-fonamide. The results suggested that p-sulfonamido-benzoic acid was the best compound for inhibitor studies in vivo. Alternatively benzene-, p-toluene, naphthalene-, or thiophene-2-sulfonamide might be preferable.