CARBONIC-ANHYDRASE INHIBITORS .43. SCHIFF-BASES DERIVED FROM AROMATICSULFONAMIDES - TOWARDS MORE SPECIFIC INHIBITORS FOR MEMBRANE-BOUND VERSUS CYTOSOLIC ISOZYMES

Schiff bases were prepared by reaction of sulfanilamide, homosulfanila mide and p-aminoethyl-benzenesulfonamide with substituted benzene- and heterocyclic aldehydes. The compounds were characterized by standard procedures and were assayed as inhibitors of three isozymes of carboni c anhydrase (CA). Several of these new compounds showed a modest two-f old selectivity for the membrane-bound (bovine) isozyme, CA IV (bCA IV ) as compared to the cytosolic human isozymes hCA I and II, in contras t to classical inhibitors which are 17-33 times less effective against bCA IV. This greater selectivity toward bCA IV is due mainly to a dec reased potency against HCA II relative to classical inhibitors. This t ype of compound might lead to the development of low molecular weight isozyme specific CA IV inhibitors.