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• W2091268594 abstract "α‐Tocopherol (vitamin E) is an important fat‐soluble antioxidant in biological systems and, as a result of scavenging reactive oxygen, it is converted to α‐tocopherylquinone. α‐Tocopherol binds to α‐tocopherol transfer protein (αTTP) in the liver cytosol, whereas α‐tocopherylquinone does not. We found that α‐tocopherylquinone binds to a liver protein with a molecular mass of about 40 kDa that is distinct from αTTP. This α‐tocopherylquinone binding protein was purified further by multiple‐step column chromatography. Sodium dodecylsulfate‐polyacrylamide gel electrophoresis of the final preparation yielded a single band with an apparent molecular mass of 25 kDa, which microsequencing revealed was identical to glutathione‐ S ‐transferase (GST). The GST activity was inhibited in the presence of α‐tocopherylquinone, as it is by other non‐substrate ligands for GST, confirming that GST and α‐tocopherylquinone interact directly. α‐Tocopherylquinone binds to GST and may be transported to the site of metabolism or excreted in the bile as other non‐substrate ligands for GST." @default.
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• W2091268594 date "1998-10-09" @default.
• W2091268594 modified "2023-09-30" @default.
• W2091268594 title "Binding of α-tocopherylquinone, an oxidized form of α-tocopherol, to glutathione-<i>S</i>-transferase in the liver cytosol" @default.
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• W2091268594 doi "https://doi.org/10.1016/s0014-5793(98)01176-4" @default.
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