Llobell A, Lopez-Ruiz A, Peinado J, Lopez-Barea J
Departamento de Bioquímica y Biología Molecular (Veterinaria), Universidad de Córdoba, Spain.
Biochem J. 1988 Jan 1;249(1):293-6. doi: 10.1042/bj2490293.
Yeast glucose-6-phosphate dehydrogenase was inhibited by low NADPH concentrations in cell-free extracts, and de-inhibited by GSSG; extensive dialysis of the crude extract did not diminish the GSSG effect. Immunoprecipitation of glutathione reductase abolished the de-inhibition of glucose-6-phosphate dehydrogenase by GSSG. Purified glucose-6-phosphate dehydrogenase was inhibited by NADPH but not de-inhibited by GSSG, and upon addition of pure glutathione reductase GSSG completely de-inhibited the glucose-6-phosphate dehydrogenase.
在无细胞提取物中,酵母葡萄糖-6-磷酸脱氢酶受到低浓度NADPH的抑制,并被GSSG解除抑制;粗提取物的广泛透析并未减弱GSSG的作用。谷胱甘肽还原酶的免疫沉淀消除了GSSG对葡萄糖-6-磷酸脱氢酶的解除抑制作用。纯化的葡萄糖-6-磷酸脱氢酶受到NADPH的抑制,但未被GSSG解除抑制,加入纯谷胱甘肽还原酶后,GSSG完全解除了葡萄糖-6-磷酸脱氢酶的抑制。