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• W2040255026 endingPage "4176" @default.
• W2040255026 startingPage "4169" @default.
• W2040255026 abstract "Abstract One mechanism for regulation of metal binding to metallothionein (MT) involves the non‐enzymatic or enzymatic oxidation of its thiols to disulfides. Formation and speciation of oxidized MT have not been investigated in detail despite the biological significance of this redox biochemistry. While metal ion‐bound thiols in MT are rather resistant towards oxidation, free thiols are readily oxidized. MT can be partially oxidized to a state in which some of its thiols remain reduced and bound to metal ions. Analysis of the oxidation products with SDS‐PAGE and a thiol‐specific labeling technique, employing eosin‐5‐iodoacetamide, demonstrates higher‐order aggregates of MT with intermolecular disulfide linkages. The polymerization follows either non‐enzymatic or enzymatic oxidation, indicating that it is a general property of oxidized MT. Supramolecular assemblies of MT add new perspectives to the complex redox and metal equilibria of this protein." @default.
• W2040255026 created "2016-06-24" @default.
• W2040255026 creator A5000431856 @default.
• W2040255026 creator A5023467794 @default.
• W2040255026 date "2008-11-01" @default.
• W2040255026 modified "2023-10-18" @default.
• W2040255026 title "Partial oxidation and oxidative polymerization of metallothionein" @default.
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• W2040255026 doi "https://doi.org/10.1002/elps.200700922" @default.
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