Abstract
In the last several years, several investigators have reported that the tocopheroxy radical, the initial product of the reaction of vitamin E (alpha-tocopherol), is recycled back to alpha-tocopherol in the course of its function as an antioxidant in biological membranes (1–3). However, direct evidence for such a process has not been provided, and the mechanism by which such a reaction could be mediated was not known. Some of the evidence which tends to support this idea was based on observations that lipid peroxidation in liver microsomes from tocopherol-deficient rats is poorly inhibited by glutathione (GSH), but is markedly inhibited by GSH in microsomes from tocopherol-sufficient rats (A). Burk and coworkers (5–7) have shown that a heat-labile factor is present in microsomes which, in the presence of GSH, prevents lipid peroxidation in these membranous particles under conditions which promote vigorous lipid peroxidation in the absence of GSH. The activity of this heat-labile, membrane-bound factor was shown to be heat-labile and destroyed by trypsin, and, therefore, presumably a constitutive protein in the microsomal membrane.
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© 1987 Plenum Press, New York
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McCay, P.B., Lai, E.K., Brueggemann, G., Powell, S.R. (1987). A Biological Antioxidant Function for Vitamin E: Electron Shuttling for a Membrane-Bound “Free Radical Reductase”. In: Galli, C., Fedeli, E. (eds) Fat Production and Consumption. NATO ASI Series, vol 131. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9495-6_15
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DOI: https://doi.org/10.1007/978-1-4615-9495-6_15
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