Abstract
Glucose 6-phosphate dehydrogenase (G6PD) was purified from buffalo ( Bubalus bubalis) erythrocytes and some characteristics of the enzyme were investigated. The purification procedure was composed of two steps: hemolysate preparation and 2 ′,5 ′-ADP–Sepharose 4B affinity gel chromatography. Thanks to the two consecutive procedures, the enzyme, having a specific activity of 69.7 EU/mg proteins, was purified 650-fold with a yield of 31%. Optimal pH, stable pH, optimal temperature, molecular weight, and K M and V max values for NADP + and glucose 6-phosphate (G6-P) substrates were also determined for the enzyme. In addition, K i values and the type of inhibition were determined by means of Lineweaver–Burk graphs obtained for such inhibitors as ATP, ADP, NADPH, and NADH.
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