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. 1980 Jul 15;190(1):125–130. doi: 10.1042/bj1900125

Role of cytoplasmic thioltransferase in cellular regulation by thiol-disulphide interchange.

B Mannervik, K Axelsson
PMCID: PMC1162070  PMID: 7447929

Abstract

Cytoplasmic thioltransferase purified from rat liver [Axelsson, Eriksson & Mannervik (1978) Biochemistry 17, 2978--2984] catalyses the formation and decomposition of mixed disulphides of proteins and glutathione. The enzyme was found to catalyse the reversible thiol-disulphide interchange between glutathione disulphide and a crude thiol-containing protein fraction from rat liver. This finding indicates a role of the thioltransferase in the regulation of the 'glutathione status' of the cell. Specifically, it was found that thioltransferase catalyses the reactivation of pyruvate kinase from rat liver that had previously been inactivated by glutathione disulphide. It is suggested that thioltransferase may have a general role in regulatory processes involving thiol-disulphide interchange.

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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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