Effects of some drugs on hepatic glucose 6-phosphate dehydrogenase activity in Lake Van Fish ( Chalcalburnus Tarischii Pallas, 1811)

Inhibitory effects of some drugs on hepatic glucose 6-phosphate dehydrogenase from Lake Van fish ( chalcalburnus tarischii pallas, 1811) were investigated. For this purpose, initially liver glucose 6-phosphate dehydrogenase was purified 899-fold in a yield of 46.24% by using 2′,5′-ADP Sepharose 4B affinity gel. In order to control the purification of enzyme was done SDS polyacrylamide gel electrophoresis. SDS polyacrylamide gel electrophoresis showed a single band for enzyme. A constant temperature (+4 °C) was maintained during the purification process. Enzyme activity was determined with the Beutler method by using a spectrophotometer at 340 nm. Vankomycine, sulfanylamide, sulfanylacetamide, nidazole, ciprofloxacin, amoxicillin and KMnO 4 were used as drugs. These drugs exhibited inhibitory effects on the enzyme. IC 50 values of vankomycine, sulfanylamide, sulfanylacetamide, nidazole, ciprofloxacin, amoxicillin and KMnO 4 were 1.88, 0.037, 0.032, 1.178, 2.26, 643.5 and 0.0002 mM, and the K i constants 1.18 ± 0.148, 0.119 ± 0.021, 0.075 ± 0.015, 1.15 ± 0.21, 7.69 ± 0.67, 1007 ± 69, and 0.001 ± 0.00022 mM, respectively. While vankomycine and nidazole showed competitive inhibition, others displayed noncompetitive inhibition. K i constants and IC 50 values for drugs were determined by Lineweaver–Burk graphs and plotting activity percentage versus [ I], respectively.