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- W1963568114 abstract "Sulindac, a sulfoxide with antiinflammatory activity, is reduced to the corresponding sulfide by rat hepatic cytosolic enzymes requiring NADPH for maximal activity. This reaction is inhibited by insulin, L-cystine, glutathione disulfide and 5,5′-dithiobis(2-nitrobenzoic acid), all of which are known to interact with the thioredoxin system comprised of NADPH, thioredoxin reductase and thioredoxin. Sodium arsenite, a known inhibitor of thioredoxin reductase, also inhibited sulindac reduction. Rat hepatic cytosolic fractions from which thioredoxin had been removed by chromatography on Sephadex G-50 showed minimal sulfoxide reductase activity; activity could be restored by addition of purified Escherichiacoli thioredoxin or dithiothreitol. These findings are the first demonstration of thioredoxin-dependent sulfoxide reduction by mammalian tissues." @default.
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- W1963568114 date "1980-12-01" @default.
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- W1963568114 title "Involvement of thioredoxin in sulfoxide reduction by mammalian tissues" @default.
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- W1963568114 doi "https://doi.org/10.1016/0006-291x(80)91454-0" @default.
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