Investigation of the inhibitory effects of some natural substances on human carbonic anhydrase I and II isoenzymes

Carbonic anhydrases (CAs) are metaloenzymes that catalyze the reaction between carbon dioxide and water. In this our aim was to examine the effects ofcertain natural substances on the purified derivates of human carbonic anhydrase 1 and 2 that were collected from human red blood cells. For this purpose firstly carbonic anhydrase isoenzymes were isolated from fresh blood using Sepharose-4B-L-tyrosine sülfanilamide colon chromatography. Carbonic anhydrases were purified 98.92 and 438.85 fold and obtained with a yield of %69.6 and %44.12 respectively. Subsequently, the inhibitory effects of derivatives of natural compounds on human carbonic anhydrase isoenzymes were investigated using esterase activity to find IC50 values, and (%) activity graphics were plotted. Using the data obtained from the graphics, the IC50 values for hCA I and hCA II of natural substances 1-5 were calculated. The IC50 values for hCA I and II are in the range of 0.0955-1.055 µM and 0.1566-0.760 µM, respectively.