期刊
ELECTROPHORESIS
卷 29, 期 20, 页码 4169-4176出版社
WILEY
DOI: 10.1002/elps.200700922
关键词
Metallothionein; Polymerization; Redox; SDS-PAGE; Thiol-reactive probes
资金
- Endowment for Research in Human Biology and National Institutes of Health [GM 065388]
- German Academic Exchange Service (DAAD)
one mechanism for regulation of metal binding to metallothionein (MT) involves the nonenzymatic 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.
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