Purification and characterization of glutathione S transferase from pearl mullet's gill of Van Lake's fish (Chalcalburnustarichi), examination of somemetals and pesticidies' effects of enzyme activity

In this study, glutathione S-transferase(E.C 1.8.1.7; GST) enzym from Van Lake pearl mullet fish refinied using glutathione agarose affinitychromatography with a spescific activity of 11344.83 EU / mg protein and 82.25 % efficiency1543.51 fold purified. SDS-polyacrylamide gel electrophoresis was performed on the purpuse of checking the purity of the purified enzyme and a single band was obtained. The molecular mass was found to be approximately 32.218 kDa. Optimum pH in the K-Phosphate was 7.3, optimum ionic strength was 120 mM K-Phosphate, optimum temperature was 35 ° C, for the enzyme and stable pH was found in the K-phosphate buffer at pH 8.0. Also for CDNB, the KM constant was 1.0574 mM and the Vmax value was 0.373 EU / ml; For GSH, the KM constant was 0.1590 mM and the Vmax value was 0.0854 EU / ml. The effects of some metal ions and pesticides of Van Lake pearl mullet's gill. Enzyme were investigated and B3+, Ba2+ , Al3+and Se2- ions which show effect of inhibition and valves of IC50 and Ki constantsare calculated for Oxamyl, Diniconazole, Carbofuran, Tebuconazole and Atrazine pesticides.