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本文引用的文献

1
Nitrate Reductase from Monoraphidium braunii: Immunocytochemical Localization and Immunological Characterization.单极藻硝酸还原酶：免疫细胞化学定位与免疫学特性。
Plant Physiol. 1985 Jul;78(3):614-8. doi: 10.1104/pp.78.3.614.
2
Protein measurement with the Folin phenol reagent.使用福林酚试剂进行蛋白质测定。
J Biol Chem. 1951 Nov;193(1):265-75.
3
A critical appraisal of the effect of oxidized glutathione on hepatic glucose 6-phosphate dehydrogenase activity.氧化型谷胱甘肽对肝脏葡萄糖-6-磷酸脱氢酶活性影响的批判性评价。
Biochem J. 1983 Sep 15;214(3):959-65. doi: 10.1042/bj2140959.
4
Reversible inactivation of Saccharomyces cerevisiae glutathione reductase under reducing conditions.在还原条件下酿酒酵母谷胱甘肽还原酶的可逆失活
Arch Biochem Biophys. 1984 Jan;228(1):1-12. doi: 10.1016/0003-9861(84)90040-7.
5
The redox state of free nicotinamide-adenine dinucleotide phosphate in the cytoplasm of rat liver.大鼠肝脏细胞质中游离烟酰胺腺嘌呤二核苷酸磷酸的氧化还原状态
Biochem J. 1969 Dec;115(4):609-19. doi: 10.1042/bj1150609a.
6
Regulation of the pentose phosphate cycle.磷酸戊糖途径的调节
Biochem J. 1974 Mar;138(3):425-35. doi: 10.1042/bj1380425.
7
The effect of oxidized glutathione on NADPH inhibition of glucose-6-phosphate dehydrogenase is indirect.氧化型谷胱甘肽对NADPH抑制葡萄糖-6-磷酸脱氢酶的作用是间接的。
Biochem J. 1985 Nov 1;231(3):806-7. doi: 10.1042/bj2310806.
8
Redox interconversion of Escherichia coli glutathione reductase. A study with permeabilized and intact cells.大肠杆菌谷胱甘肽还原酶的氧化还原互变。对透化细胞和完整细胞的研究。
Mol Cell Biochem. 1985 Oct;68(2):121-30. doi: 10.1007/BF00219376.
9
The redox interconversion mechanism of Saccharomyces cerevisiae glutathione reductase.酿酒酵母谷胱甘肽还原酶的氧化还原互变机制
Eur J Biochem. 1985 Sep 2;151(2):275-81. doi: 10.1111/j.1432-1033.1985.tb09097.x.
10
Regulation of the pentose phosphate cycle. Cofactor that controls the inhibition of glucose-6-phosphate dehydrogenase by NADPH in rat liver.磷酸戊糖途径的调节。控制大鼠肝脏中NADPH对葡萄糖-6-磷酸脱氢酶抑制作用的辅助因子。
Biochem J. 1986 Nov 1;239(3):553-8. doi: 10.1042/bj2390553.

谷胱甘肽还原酶直接介导了谷胱甘肽二硫化物对酵母葡萄糖-6-磷酸脱氢酶的刺激作用。

Glutathione reductase directly mediates the stimulation of yeast glucose-6-phosphate dehydrogenase by GSSG.

作者信息

Llobell A, Lopez-Ruiz A, Peinado J, Lopez-Barea J

机构信息

Departamento de Bioquímica y Biología Molecular (Veterinaria), Universidad de Córdoba, Spain.

出版信息

Biochem J. 1988 Jan 1;249(1):293-6. doi: 10.1042/bj2490293.

DOI:10.1042/bj2490293
PMID:3277619
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1148696/
Abstract

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.

摘要

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。