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Reduction of the selenotrisulfide derivative of glutathione to a persulfide analog by glutathione reductase.

作者信息

Ganther H E

出版信息

Biochemistry. 1971 Oct 26;10(22):4089-98. doi: 10.1021/bi00798a013.

DOI:10.1021/bi00798a013
PMID:4400818
Abstract
摘要

相似文献

1
Reduction of the selenotrisulfide derivative of glutathione to a persulfide analog by glutathione reductase.
Biochemistry. 1971 Oct 26;10(22):4089-98. doi: 10.1021/bi00798a013.
2
Circular dichroism of reduced and oxidized mammalian lipoamide dehydrogenase.还原型和氧化型哺乳动物硫辛酰胺脱氢酶的圆二色性
J Biol Chem. 1971 Sep 10;246(17):5498-503.
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Identification of the thiol residues involved in modifications of pig heart lipoamide dehydrogenase by cupric ion and by iodoacetamide.鉴定猪心脂酰胺脱氢酶被铜离子和碘乙酰胺修饰过程中涉及的巯基残基。
Biochim Biophys Acta. 1974 Nov 25;370(1):39-48. doi: 10.1016/0005-2744(74)90029-1.
4
Synthesis and some reactions of the pantetheine-glutathione mixed disulfide.泛酰巯基乙胺 - 谷胱甘肽混合二硫键的合成及一些反应
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5
Enzymatic catalysis of the reversible sulfitolysis of glutathione disulfide and the biological reduction of thiosulfate esters.谷胱甘肽二硫化物可逆亚硫酸解的酶促催化作用及硫代硫酸酯的生物还原作用。
Arch Biochem Biophys. 1974 Jul;163(1):283-9. doi: 10.1016/0003-9861(74)90478-0.
6
Interconversion of the multiple forms of dihydrofolate reductase from amethopterin-resistant Lactobacillus casei.来自氨甲蝶呤抗性干酪乳杆菌的二氢叶酸还原酶多种形式的相互转化。
Biochem Biophys Res Commun. 1971 Mar 5;42(5):772-7. doi: 10.1016/0006-291x(71)90495-5.
7
Di- -glutamylcystine as a substrate for glutathione reductase.二谷胱甘肽作为谷胱甘肽还原酶的底物。
Biochim Biophys Acta. 1971 Jul 21;242(1):36-8. doi: 10.1016/0005-2744(71)90085-4.
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Characterization of porcine malate dehydrogenase. II. Amino acid sequence of a peptide containing the active center histidine residue.猪苹果酸脱氢酶的特性研究。II. 包含活性中心组氨酸残基的肽段的氨基酸序列。
Biochim Biophys Acta. 1974 Jun 7;351(2):295-300.
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Isolation and characterization of glutathione reductase from Penicillium chrysogenum.产黄青霉谷胱甘肽还原酶的分离与鉴定
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10
Selenotrisulfides. II. Cross-linking of reduced pancreatic ribonuclease with selenium.硒代三硫化物。II. 还原型胰核糖核酸酶与硒的交联作用
Biochemistry. 1969 Jun;8(6):2557-63. doi: 10.1021/bi00834a044.

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