Purification, characterization and determination of inhibition with some natural moleculars of bovine renal carbonic anhydrase enzyme

The carbonic anhydrase (CA) (E.C. 4.2.1.1) enzyme is a very important enzyme that reversibly catalyzes the conversion of HCO3- and H+ to hydration of CO2 in almost all living organisms. In this study, a newly synthesized benzylcellulose-sulfanilamide affinity gel was used for the purification of the bovine kidney carbonic anhydrase enzyme. In the second part of the study, the inhibitory effects of some natural substances (quarcetin, catechin, chlorogenic acid, abscisic acid, morin and routine) on the purified and characterized CA enzyme were investigated. For this purpose, IC50 values were calculated for these natural hydroxylic substances which have an inhibitory effect on enzyme activities.