Improved purification and sulfhydryl analysis of thiosulfate reductase

作者: Thomas R. Chauncey , John Westley

DOI: 10.1016/0167-4838(83)90204-2

关键词: CysteineStereochemistryDithionitrobenzoic AcidSulfurtransferaseIodoacetamideBond cleavageAmino acidThiosulfateChemistryGlutathioneBiochemistry

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.

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