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  • Title: The substrate-mediated inactivation of the pyruvate dehydrogenase component of the pigeon breast muscle pyruvate dehydrogenase complex.
    Author: Khailova LS, Nemerya NS, Severin SE.
    Journal: Biochem Int; 1983 Oct; 7(4):423-32. PubMed ID: 6679739.
    Abstract:
    Incubation of the pyruvate dehydrogenase component isolated from the pigeon breast muscle pyruvate dehydrogenase complex with Mg2+, thiamine pyrophosphate and low concentrations of pyruvic acid in the absence of electron acceptors results in irreversible time-dependent inactivation of the enzyme. The rate of the enzyme inactivation is markedly decreased in the presence of high concentrations of pyruvate; in this case acetoin and acetolactate are detected in the reaction mixture. The enzyme activity is stabilized when the artificial electron acceptor, 2,6-dichlorophenolindophenol, is present in the reaction mixture. The substrate-mediated inactivation of the enzyme is accompanied by incorporation of the 2-[14C]-substrate fragment and labelled thiamine pyrophosphate into the protein fraction. The enzyme reactivation by neutral hydroxylamine and the protective effect of dithiothreitol suggest that the SH-group(s) may be involved in the substrate-mediated inactivation of pyruvate dehydrogenase.
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