Examination of antiglaucoma activity on novel proton transfer compounds

In this study, the effects of purificatin of carbonic anhydrase enzyme from human erythrocyte and previously synthesized compounds on HCA I and HCA II that carry out roles on the treatment of glaucoma were investigated in vitro.First, erythrocyte carbonic anhydrase isoenzymes (HCA I, HCA II) from human erythrocyte were separately purifed by using affinity chromatography and then kinetic investigations were held with these enzymes.Later inhibition effects of newly synthesized compounds (1and 2) from Hsba and free ligands (en and amp) on human erythrocyte HCA enzymses were investigated in vitro. During the examinations, hydrates and esterase activites were utilized to determine carbonic anhydrase activities. It was observed that (Hsba, 1 and 2) compounds showed inhibition effects on HCA hydratase and esterase activity. I50 values were determined by drawing %activity-[I] graphs for drugs showing inhibition effects. For CO2-hydratase activity of compounds (Hsba), (1), (2) showed inhibition effects of 0.45 ? M , 0.15 ? M and 0.32 ? M for HCA I, and 0.40 ? M, 0.06 ? M and 0.15 ? M with I50 for HCA II, respectively (with an inhibitor concentration that would drop enzymed reaction time %50). As for esterase activity of p-nitrophenyl acetate, compounds (Hsba), (1), (2) had inhibition effects of 3.2 ? M, 0.13 ? M and 0.8 ? M for HCA I and 18 ? M, 0.14 ? M ve 0.1 ? M for HCA II with I50.