Role of cytoplasmic thioltransferase in cellular regulation by thiol-disulphide interchange
- 15 July 1980
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 190 (1), 125-130
- https://doi.org/10.1042/bj1900125
Abstract
Cytoplasmic thioltransferase purified from rat liver catalyzes the formation and decomposition of mixed disulfides of proteins and glutathione. The enzyme catalyzed the reversible thiol-disulfide interchange between glutathione disulfide 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. Thioltransferase catalyzes the reactivation of pyruvate kinase from rat liver that was previously inactivated by glutathione disulfide. Thioltransferase may have a general role in regulatory processes involving thiol-disulfide interchange.This publication has 23 references indexed in Scilit:
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