Purification of Glucose 6-Phosphate Dehydrogenase From Goose Erythrocytes and Kinetic Properties

Authors : Şükrü BEYDEMİR

Pages : 1179-1185

View : 20 | Download : 8

Publication Date : 0000-00-00

Article Type : Research Paper

Abstract :Glucose 6-phosphate dehydrogenase insert ignore into journalissuearticles values(G6PD); was purified from goose erythrocytes and some characteristics of the enzyme were investigated. The purification procedure was composed of 3 steps: hemolysate preparation, ammonium sulfate precipitation, and 2`, 5`-ADP Sepharose 4B affinity gel chromatography. Thanks to the 3 consecutive procedures, the enzyme, having a specific activity of 36.2 EU/mg protein, was purified for a yield of 68.79% and 3892 folds; to ascertain enzyme purity, SDS-PAGE was performed. Optimal pH, stable pH, optimal temperature, molecular weight, and Km and Vmax values for NADP+ and glucose 6-phosphate insert ignore into journalissuearticles values(G6-P); substrates were also determined for the enzyme. In addition, Ki values and inhibition type were determined by means of Lineweaver-Burk graphs obtained for such inhibitors as ATP, ADP and NADPH. These materials inhibited the enzyme in a noncompetitive manner.
Keywords : Goose, purification, glucose 6 phosphate dehydrogenase, erythrocyte