Purification and properties of the Ascaris pyruvate dehydrogenase complex.
Biochim Biophys Acta
; 571(1): 1-11, 1979 Nov 09.
Article
en En
| MEDLINE
| ID: mdl-227453
ABSTRACT
The pyruvate dehyhdrogenase complex (pyruvatelipoate oxidoreductase (decarboxylating and acceptor-acetylating), EC 1.2.4.1) has been isolated from Ascaris muscle mitochondria and purified to near homogeneity by differential centrifugation, (NH4)2SO4 fractionation and calcium phosphate gel-cellulose chromatography. It is similar in shape, size and physical characteristics to pyruvate dehydrogenase complexes isolated from mammalian sources. It has an absolute dependence on CoA, NAD+ and pyruvate for activity and is competitively inhibited by acetyl-CoA and NADH. However, much higher NADH/NAD+ ratios are necessary to inhibit activity, suggesting regulation by the more reduced state of the pyridine nucleotide pool in Ascaris mitochondria.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Ascaris
/
Complejo Piruvato Deshidrogenasa
Límite:
Animals
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1979
Tipo del documento:
Article