Abstract
The protecting effect of selenium against the toxicity of methylmercury (MM) and mutual Se-Hg antagonism has long been known. The defensive action of Se does not occur by greater Hg body excretion but by a rearrangement in the accumulation pattern of Hg in organs. According to some authors, the Se-Hg interaction is brought about by endogenous glutathione (GSH) which in reducing selenite to selenide favors the formation of bis-methylmercury selenide. The high lipoaffinity of this compound alters the metabolism and distribution of mercury in critical tissues and thus its toxicity. The function of GSH as a protective agent against MM toxicity has recently been confirmed. GST is an important family of isozenzymes with binding properties which metabolize drugs and xenobiotics. These enzymes could indeed have an important function in Se-Hg antagonism. Their participation in conjugation with GSH and bile excretion of MM has been suggested by Refsvik although other authors seem to exclude it. In the present paper the behavior of GST isoenzymes in quail liver after combined Se-Hg treatment was studied; in addition other enzymes which regulate the GSH metabolism as well as the hapatic levels of Se, Hg, GSH and oxidized glutathione (GSSG) have been investigated.
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