Yilmaz, HÇiftçi, MBeydemir, SBakan, EKüfrevioglu, ÖI2024-04-242024-04-2420030301-12080975-0959https://hdl.handle.net/11468/21228Glucose 6-phosphate dehydrogenase (G6PD) was purified from turkey erythrocytes by ammonium sulphate precipitation and followed by ADP Sepharose affinity gel chromatography. The yield was 49.71% and specific activity of the enzyme was found to be 4.4.16 EU/mg protein. By gel filtration the molecular mass was found to be 75 kDa. The enzyme had an optimum pH at 9.0, and opt;mum temperature at 50degreesC. K-m and V-max for NADP(+) and glucose 6- phosphate (G6-P) as substrates were also determined and effects of inhibitors such as ATP, NADH and NADPH were examined.eninfo:eu-repo/semantics/closedAccess[No Keyword]Article4016265WOS:0001812990000102-s2.0-003820183122900294Q3Q4