Open AccessRise of Coenzyme A‐Glutathione Mixed Disulfide during Hydroperoxide Metabolism in Perfused Rat Liver
Author(s) -
CRANE Denis,
HÄUSSINGER Dieter,
SIES Helmut
Publication year - 1982
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1982.tb06911.x
Subject(s) - glutathione , glutathione disulfide , chemistry , coenzyme a , metabolism , glutathione peroxidase , cofactor , selenium , disulfide bond , endocrinology , medicine , biochemistry , peroxidase , enzyme , biology , reductase , organic chemistry
The hepatic metabolism of an externally added hydroperoxide, t ‐butyl hydroperoxide, results in substantial decreases in CoASH and acetyl‐CoA and a concomitant increase in CoA‐disulfides. The principal CoA‐disulfide which is formed under these conditions was identified as CoASSG, the mixed disulfide of coenzyme A and glutathione; CoASSCoA levels were unchanged. The perturbation in the coenzyme A system was absent when the hydroperoxide was infused into livers from rats maintained on a selenium‐deficient diet. In these livers, Se‐dependent glutathione peroxidase is lowered to less than 5% of control levels; the observed effects can be attributed to flux through Se‐dependent GSH peroxidase.