Investigation of inhibition effect of 4-methylbenzenesulfonamide derivatives on human carbonic anhydrase isoenzymes (hCA I-II)

Carbonic anhydrases (CAs) are metaloenzymes that catalyze the reaction between carbon dioxide and water. In this study, it was aimed to investigate the purification of hCA I and hCA II isoenzymes from human erythrocytes and the effects of certain 4-methylbenzenesulfonamide derivatives on the esterase activity of enzymes. For this purpose, firstly, hCA I and hCA II isoenzymes were purified from human fresh blood by Sepharose-4B-L-tyrosine sülfanilamide affinity colon chromatography. The hCA I and hCA II isoenzymes were purified 97,05 and 468,90 fold and obtained with %67,82, %49,27 yield, respectively. Subsequently, the inhibitory effects of sulfonamide derivatives on human carbonic anhydrase isoenzymes I and II were investigated using esterase activity and plotted (%) Activity-[Sulfonamide] graphs to find IC50 values. Utilizing the obtained graphs, IC50 values for hCA I and hCA II of the 1-9 numbered sulfonamide derivatives were found. The IC50 values for hCA I-II are in the range of 0,770-5,196 nM and 18,887-56,862 nM, respectively.