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Glutathione disulfide enhances the reduced glutathione inhibition of lipid peroxidation in rat liver microsomes.

Abstract：

:Experiments were undertaken to examine the effects of reduced (GSH) and oxidized (GSSG) glutathione on lipid peroxidation of rat liver microsomes. Dependence on microsomal alpha-tocopherol was shown for the GSH inhibition of lipid peroxidation. However, when GSH (5 mM) and GSSG (2.5 mM) were combined in the assay system, inhibition of lipid peroxidation was enhanced markedly over that with GSH alone in microsomes containing alpha-tocopherol. Surprisingly, the synergistic inhibitory effect of GSH and GSSG was also observed for microsomes that were deficient in alpha-tocopherol. These data suggest that there may be more than one factor responsible for the glutathione-dependent inhibition of lipid peroxidation. The first is dependent upon microsomal alpha-tocopherol and likely requires GSH for alpha-tocopherol regeneration from the alpha-tocopheroxyl radical during lipid peroxidation. The second factor appears to be independent of alpha-tocopherol and may involve the reduction of lipid hydroperoxides to their corresponding alcohols. One, or possibly both, of these factors may be activated by GSSG through thiol/disulfide exchange with a protein sulfhydryl moiety.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Scholz RW,Graham KS,Reddy CC

doi

10.1016/0006-291x(90)90904-2

subject

Has Abstract

pub_date

1990-01-30 00:00:00

pages

960-6

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(90)90904-2

journal_volume

166

pub_type

杂志文章

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