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. 1975 Sep;149(3):785–788. doi: 10.1042/bj1490785

Reduction of disulphide bonds in proteins mixed disulphides catalysed by a thioltransferase in rat liver cytosol.

B Mannervik, K Axelsson
PMCID: PMC1165689  PMID: 1201003

Abstract

The reduction of mixed disulphides of some proteins and GSH [Protein(-SSG)n] is accomplished with GSH as a reductant and a thioltransferase from rat liver as a catalyst, thus: See article. The spontaneous reaction is negligible in comparison with the enzymic reaction in vivo, and any direct reduction with glutathione reductase is not detectable with the substrates used. The reduction is only indirectly dependent on NADPH, which is required for the regeneration of GSH from GSSG. Other protein disulphides apparently are reduced via analogous GSH-dependent reactions

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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