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. 1985 Jun 15;228(3):661–665. doi: 10.1042/bj2280661

Selective reduction of a disulphide bridge in hen ovotransferrin.

J Williams, K Moreton, A D Goodearl
PMCID: PMC1145035  PMID: 4026802

Abstract

Brief treatment of iron-saturated hen ovotransferrin with dithiothreitol selectively cleaves the disulphide bridge between residues 478 and 671, which is in the C-terminal domain of the protein. The reduced alkylated protein is less stable than the native protein, and its iron-binding properties are different. A fluorescent derivative was prepared by coupling N-iodoacetyl-N'-(5-sulpho-1-naphthyl)ethylenediamine to the thiol groups.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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