Abstract
Glutathione (GSH), a multifunctional tripeptide thiol found in virtually all mammalian cells, has a prominent role in the maintenance and execution of many homeostatic and regulatory processes of the cell (1). Of the many functions of GSH, perhaps the most studied, is its ability to protect the cell against the detrimental effects of ionizing radiation, reactive oxygen compounds, free radicals, and toxic xenobiotics (2). The GSH oxidation-reduction cycle is of primary importance when dealing with reactive oxygen intermediates as well as the detoxification of xenobiotics. Although the elimination of each is catalyzed by different enzymes, GSH peroxidase in the former and GSH S-transferases in the latter, the maintenance of a high ratio of GSH:GSSG by the cycle is of vital importance to both pathways.
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© 1987 Plenum Press, New York
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Messina, J.P., Mazurkiewicz, J., Lawrence, D.A. (1987). Production and Characterization of Monoclonal Antibodies to Thiol-Modified Glutathione. In: Cerutti, P.A., Nygaard, O.F., Simic, M.G. (eds) Anticarcinogenesis and Radiation Protection. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-6462-1_61
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DOI: https://doi.org/10.1007/978-1-4615-6462-1_61
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