| 6513990 |
Takamiya S, Furushima R, Oya H: Electron transfer complexes of Ascaris suum muscle mitochondria: I. Mol Biochem Parasitol. 1984 Oct;13(2):121-34.
Characterization of NADH-cytochrome c reductase (complex I-III), with special reference to cytochrome localization.. An NADH-cytochrome c reductase (complex I-III) was isolated from Ascaris suum muscle mitochondria. The enzyme preparation catalyzed the reduction of 1.68 mumol cytochrome c min-1 mg-1 protein at 25 degrees C with NADH but not with NADPH, and retained its sensitivity to rotenone, piericidin A and 2-heptyl-4-hydroxyquinoline-N-oxide as with the submitochondrial particles. The isolated complex I-III, essentially free of succinate-cytochrome c reductase and cytochrome c oxidase, consisted of fourteen polypeptides with apparent molecular weights ranging from 76 000 to 12 000. The complex I-III contained three cytochromes, b-559.5, b-563 and c1-550.5 and Pigment-558 at concentrations of 1.28, 0.211, 1.23 and 0.321 nmol mg-1 protein, respectively. Cytochrome b-558, a major constituent cytochrome of Ascaris mitochondria and previously suggested to participate in the fumarate reductase system, was not fractionated in the complex I-III. Localization of the cytochromes in Ascaris electron transfer complexes is discussed. |
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