Rise of coenzyme A-glutathione mixed disulfide during hydroperoxide metabolism in perfused rat liver.
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.
D000105:Acetyl Coenzyme A / Q000378:metabolism; D000818:Animals; D003065:Coenzyme A / Q000031:analogs & derivatives* / Q000378:metabolism; D005979:Glutathione Peroxidase / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism*; D066298:In Vitro Techniques; D008099:Liver / Q000378:metabolism*; D008297:Male; D010477:Perfusion; D051381:Rats; D011919:Rats, Inbred Strains
C019305:coenzyme A-glutathione mixed disulfide; D000105:Acetyl Coenzyme A; D006861:Hydrogen Peroxide; D005979:Glutathione Peroxidase; D003065:Coenzyme A