Yilmaz Hayrullah, Ciftçi Mehmet, Beydemir Sükrü, Bakan Ebubekir, Küfrevioğlu O Irfan
Dicle University, Faculty of Education, Department of Chemistry.
Indian J Biochem Biophys. 2003 Feb;40(1):62-5.
Glucose 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 44.16 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 optimum temperature at 50 degrees C. Km and Vmax 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.
通过硫酸铵沉淀，随后进行ADP琼脂糖亲和凝胶色谱法，从火鸡红细胞中纯化出葡萄糖6-磷酸脱氢酶（G6PD）。产率为49.71%，发现该酶的比活性为44.16酶活力单位/毫克蛋白质。通过凝胶过滤法测得分子量为75 kDa。该酶的最适pH为9.0，最适温度为50℃。还测定了以NADP(+)和葡萄糖6-磷酸（G6-P）为底物时的米氏常数（Km）和最大反应速度（Vmax），并研究了ATP、NADH和NADPH等抑制剂的影响。
