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Reactions of unsymmetrical disulfides:II. Sulfitolysis of disulfide bonds linking proteins to small molecules

Authors
Journal
Archives of Biochemistry and Biophysics
0003-9861
Publisher
Elsevier
Publication Date
Volume
121
Issue
3
Identifiers
DOI: 10.1016/0003-9861(67)90060-4
Disciplines
  • Biology

Abstract

Abstract The reactions of sulfite on the mixed disulfides of glutathione and cysteine and on those of thiol-proteins and cysteine have been investigated. It was found that substitution at the S-S bond of the glutathione-cysteine disulfide takes place at random but that a specific sulfur atom (that of the “free” cysteine part of the molecule) in the protein-cysteine mixed disulfides is attacked more frequently than its mate. This directed substitution is eliminated when the reaction is carried out in a concentrated solution of urea.

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