Chesnokova L S
Eksp Onkol. 1990;12(3):68-70.
The properties of glucose-6-phosphate dehydrogenase (G6PDH; glucose-6-phosphate-NADP-oxidoreductase, EC 1.1.1.49) in the liver tissue of intact rats and those with ascites Zaidel hepatoma were compared. The specific activity of the enzyme from hepatoma was 7 times as high as that of the enzyme from the normal liver. The G6PDH preparations with the specific activity of 1.5 U/mg of protein were obtained by the three-stage purification. No differences in kinetic properties, coenzyme specificity and electrophoretic mobility of the enzymes from hepatoma and normal liver were observed.
比较了完整大鼠及患有扎伊德尔腹水肝癌大鼠肝脏组织中葡萄糖-6-磷酸脱氢酶(G6PDH;葡萄糖-6-磷酸-NADP-氧化还原酶,EC 1.1.1.49)的特性。肝癌组织中该酶的比活性是正常肝脏中该酶比活性的7倍。通过三步纯化获得了比活性为1.5 U/mg蛋白质的G6PDH制剂。未观察到肝癌组织和正常肝脏组织中该酶在动力学特性、辅酶特异性和电泳迁移率方面的差异。