Ketoprofenin 6-Fosfoglukonat Dehidrogenaz Aktivitesi Üzerine In Vitro ve In Vivo Etkisinin Araştırılması

In this study, 6-phosphogluconate dehydrogenase (E.C.1.1.1.44; 6PGD) was purified in human erythrocytes. This process was carried out by the preparation of hemolysate, precipitation by (NH4)2SO4 and 2',5'-ADP Sepharose 4B affinity chromatography . The degree of purity of the enzyme was determined with SDS-PAGE electrophoresis. The effect of ketoprofen on the enzyme was investigated in vitro and in vivo. Human erythrocyte 6PGD was purified in 742-fold at the end of all purification processes. The recovery of 6PGD was 50%, and its specific activity was 0.46U/mg in erythrocytes. Enzyme activity was spectrophotometrically measured using the Beutler method at 340 nm. Ketoprofen inhibited the enzyme activity in in vitro conditions. IC50 value of the drug inhibition in vitro was determined. For the drug having low IC50value (drug concentrations which produce 50% inhibition) (ketoprofen), in vivo studies were performed in New Zealand albino rabbits. In the evaluation of the in vivo effect of drug on 6PGD activity, it was observed that ketoprofen given at the first (P<0.01) and third hour (P<0.01), significantly inhibited the 6PGD activity