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. 1978 Aug 1;173(2):701–704. doi: 10.1042/bj1730701

Half-sites oxidation of bovine liver uridine diphosphate glucose dehydrogenase.

J S Franzen, P Marchetti, R Ishman, J Ashcom
PMCID: PMC1185826  PMID: 697744

Abstract

6,6-Dithiodinicotinate shows half-of-the-sites reactivity towards the six catalytic-site thiol groups of bovine liver UDP-glucose dehydrogenase. The reagent introduces three intrasubunit disulphide linkages between catalytic-site thiol groups and non-catalytic-site thiol groups and abrogates 60% of the catalytic activity of the hexameric enzyme; excess 2-mercaptoethanol rapidly restores full catalytic activity. These results show the half-of-the-sites behaviour of the enzyme with the reagent and the presence of a non-catalytic-site thiol group capable of forming a disulphide linkage with a catalytic-site thiol group on the same subunit without irreversible denaturation.

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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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