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• W2055551468 abstract "In intact human erythrocytes, SH-oxidizing agents exclusively cross-link spectrin via disulfide bonds. In ghosts, additional dimerization of the major intrinsic protein, band 3, is observed. After blockade of intracellular GSH the agents dimerize band 3 in the intact cell too, indicating that GSH may prevent band 3 dimerization under physiological conditions. The oxidizing agents reversibly oxidize 80% of the membrane SH-groups, suggesting that these groups are arranged close enough to each other to form disulfide bonds. This arrangement may protect other cell structures against free radicals or oxidative stress." @default.
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• W2055551468 date "1977-09-01" @default.
• W2055551468 modified "2023-09-24" @default.
• W2055551468 title "Intra- and intermolecular cross-linking of membrane proteins in intact erythrocytes and ghosts by SH-oxidizing agents" @default.
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• W2055551468 doi "https://doi.org/10.1016/0005-2736(77)90186-9" @default.
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