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Binding of methylmercury and methylmercury-thiol complexes by myelin isolated from mice of differing selenium status

Journal Article · · Bull. Environ. Contam. Toxicol.; (United States)
DOI:https://doi.org/10.1007/BF01607839· OSTI ID:6830483
The chemical form of methylmercury found in the body provides evidence of the intimate involvement of glutathione and glutathione metabolites with methylmercury. The involvement of glutathione in converting protein bound methylmercury to low molecular weight methylmercury-selenium compounds was shown earlier. The effectiveness of selenium in modifying mercury metabolism has attracted increasing attention. After finding that concurrent equimolar selenite injections increased the uptake of mercury but did not alter the mercury distribution in the brain and that selenium reversed the effect of mercury upon glutathione peroxidase, Prohaska and Ganther suggested a complex of mercury and selenium may be involved in the interaction of mercury and selenium. However, considering that the protective effect of selenium is exerted within the tissue without decreasing the concentration or amount of mercury in the tissue, selenium is probably not simply chelating the bulk of brain mercury. The purpose of the following experiments was to determine the binding characteristics of thiol-metabolites of methylmercury to myelin isolated from the central nervous system. The possible alteration of such binding by dietary selenium was also investigated.
Research Organization:
National Marine Fisheries Service, Charleston, SC
OSTI ID:
6830483
Journal Information:
Bull. Environ. Contam. Toxicol.; (United States), Journal Name: Bull. Environ. Contam. Toxicol.; (United States) Vol. 37:5; ISSN BECTA
Country of Publication:
United States
Language:
English