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Title: Half-sites oxidation of bovine liver uridine diphosphate glucose dehydrogenase. Author: Franzen JS, Marchetti P, Ishman R, Ashcom J. Journal: Biochem J; 1978 Aug 01; 173(2):701-4. PubMed ID: 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.[Abstract] [Full Text] [Related] [New Search]