Purification and properties of the Ascaris pyruvate dehydrogenase complex.

作者: Richard Komuniecki , Patricia R. Komuniecki , Howard J. Saz

DOI: 10.1016/0005-2744(79)90219-5

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摘要: Abstract The pyruvate dehydrogenase complex (pyruvate:lipoate oxidoreductase (decarboxylating and acceptor-acetylating), EC 1.2.4.1) has been isolated from Ascaris muscle mitochondria purified to near homogeneity by differential centrifugation, (NH4)2SO4 fractionation calcium phosphate gel-cellulose chromatography. It is similar in shape, size physical characteristics complexes mammalian sources. an absolute dependence on CoA, NAD+ for activity competitively inhibited acetyl-CoA NADH. However, much higher NADH/NAD+ ratios are necessary inhibit activity, suggesting regulation the more reduced state of pyridine nucleotide pool mitochondria.

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