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In this study, glucose 6-phosphate dehydrogenase (G6PD; EC 1.1.1.49) which is an importance enzyme for the carbohydrate metabolism, was purified from quail's erythrocyte and characterized. The purification was performed by preparation of hemolysate and 2', 5'-ADP Sepharose-4B affinity chromatography. G6PD from quail's erythrocyte was obtained with a yield of 77.17% having a specific activity of 60.40EU/mg. protein. The overall purification fold was around 4137. The characterization studies were showed: the stable pH value of enzyme to be 7.5 in Tris-HCl buffer, optimum pH value to be 8.0 in Tris-HCl buffer. The optimum temperature was found at 65oC and the optimum ionic strength at 1 M Tris-HCl. Molecular weight of G6PD enzyme from quail's erythrocyte was determined as 78.8 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Finally, the KM and Vmax values for substrate (G6P) and coenzyme (NADP+) of the G6PD enzyme were calculated. KM and Vmax values for the NADP+ coenzyme found as 0.001 mM and 0.124 EU/mL respectively, and the KM and Vmax values for G6P substrate found as 0.012 mM and 0.05 EU/mL respectively.