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Purification of Glucose 6-Phosphate Dehydrogenase Enzyme from Capoeta Umbla Kidney Tissue and Examination of The Effects of Some Antibiotics On Enzyme Activity

In this study, glucose 6-phosphate dehydrogenase (G6PD; EC 1.1.1.49) enzyme which is of great importance for the metabolism was purified from Capoeta umbla kidney tissue. The purification was performed by preparation of homogenates, ammonium sulphate precipitation and 2’,5’-ADP Sepharose 4B afinity chromatography. As a result of these procedures, the enzyme having the specific activity of 11.26 EU/mg proteins was purified 402.14-fold with a yield of 22.7 %. Enzyme purification was checked by performing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Enzyme activity was determined with the Beutler metod by using a spectrophotometer at 340 nm. Furthermore, the effects of some antibiotics (ampicillin, gentamicin, penicillin G and sefuroxime sodium) were investigated on C. umbla kidney enzyme activity. All used antibiotics indicated the inhibitory effects on the ezyme. IC 50 and K i values were calculated for this antibiotics which show inhibition effects. In conclusion, gentamicin inhibits the enzyme activity more than ampicillin, penicillin G and sefuroxime sodium. Key words: Antibiotic, Capoeta umbla, glucose 6-phosphate dehydrogenase, inhibition