Kinetic properties of the partially purified pyruvate dehydrogenase complex of ox brain - PubMed (original) (raw)

Kinetic properties of the partially purified pyruvate dehydrogenase complex of ox brain

J P Blass et al. Biochem J. 1973 Jan.

Abstract

The properties of a purified preparation of the pyruvate dehydrogenase complex from ox brain have been compared with those of a similar preparation from ox kidney. A broad pH optimum around 7.8, similar dependence on ionic strength, and independence of the nature of the buffer anions or cations characterized preparations from both tissues. Michaelis constants for the binding of pyruvate, thiamin pyrophosphate, NAD(+) and CoA were also similar. Enzyme from both tissues was inhibited by NADH, by copper and other heavy metals, by high concentrations of tricarboxylic acid-cycle intermediates, and by preincubation with ATP. Acetyl-CoA itself did not appear to inhibit these preparations, although some commercial preparations of acetyl-CoA did contain an inhibitor. Although oxaloacetate and alpha-oxobutyrate were weak inhibitors, a number of other alpha-oxo acids including phenylpyruvate did not inhibit. The properties of the pyruvate dehydrogenase complex from brain and kidney appeared similar.

PubMed Disclaimer

References

    1. Arch Biochem Biophys. 1970 Jun;138(2):653-61 - PubMed
    1. Hoppe Seylers Z Physiol Chem. 1971 Mar;352(3):447-52 - PubMed
    1. Nature. 1967 Apr 15;214(5085):276 - PubMed
    1. J Biol Chem. 1966 Oct 25;241(20):4694-9 - PubMed
    1. J Biol Chem. 1964 Jan;239:18-30 - PubMed

MeSH terms

Substances

LinkOut - more resources