Yilmaz, HCiftci, MBeydemir, SBakan, E2024-04-242024-04-2420021082-60681532-2297https://doi.org/10.1080/PB-120013475https://hdl.handle.net/11468/17088Glucose 6-phosphate dehydrogenase (G6PD) was purified from chicken erythrocytes, and some characteristics of the enzyme were investigated. The purification procedure was composed of three steps: hemolysate preparation, ammonium sulfate precipitation, and 2',5'-ADP Sepharose 4B affinity gel chromatography. Thanks to the three consecutive procedures, the enzyme, having the specific activity of 20.862 EU/mg proteins, was purified with a yield of 54.68% and 9,150-fold. Optimal pH, stable pH, optimal temperature, molecular weight, and K-M and V-max values for NADP(+) and glucose 6- phosphate (G6-P) were also determined for the enzyme. In addition, K-i values and the type of inhibition were determined by means of Line-Weaver-Burk graphs obtained for such inhibitors as ATP, ADP, NADH, and NADPH.eninfo:eu-repo/semantics/closedAccess[No Keyword]Article323287301WOS:0001785350000062-s2.0-00364037371237581610.1080/PB-120013475Q2Q4