作者: Thomas R. Chauncey , John Westley
DOI: 10.1016/0167-4838(83)90204-2
关键词: Cysteine 、 Stereochemistry 、 Dithionitrobenzoic Acid 、 Sulfurtransferase 、 Iodoacetamide 、 Bond cleavage 、 Amino acid 、 Thiosulfate 、 Chemistry 、 Glutathione 、 Biochemistry
摘要: Thiosulfate reductase purified 900-fold from an extract of baker's yeast by a new procedure consisted three charge-isomeric species, all with catalytic activity. Amino acid analysis thiosulfate and titrations 5,5'-dithiobis(2-nitrobenzoate) iodo[14C]acetate indicated only one cysteine residue per enzyme molecule. Alkylation this either iodoacetate or iodoacetamide did not inactivate the enzyme, indicating that sulfur-sulfur bond cleavage in substrate does require enzymic sulfhydryl group as attacking nucleophile.