Cytochrome c oxidase from bakers' yeast. Photolabeling of subunits exposed to the lipid bilayer.

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Cytochrome c Oxidase from Bakers’ Yeast

Purified cytochrome c oxidase from bakers’ yeast can be resolved into six polypeptide bands by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The apparent molecular weights of these components are I, 42,000; II, 34,500; III, 23,000; IV, 14,000; V, 12,500; and VI, 9,500. (Although Component V actually consists of two distinct polypeptide species, it will be regarde...

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Cytochrome c Oxidase from Bakers’ Yeast

Cytochrome aa3 was purified 35to 40-fold from submitochondrial particles of commercial bakers’ yeast. The purification procedure involved solubilization of the enzyme with cholate, fractionation with ammonium sulfate, and chromatography on DEAE-cellulose in the presence of Triton x-100. The purified, active enzyme contained approximately 10 nmoles of heme a per mg of protein and was free of oth...

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Cytochrome c oxidase from bakers' yeast. II. Site of translation of the protein components.

Purified cytochrome c oxidase from bakers’ yeast can be resolved into six polypeptide bands by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The apparent molecular weights of these components are I, 42,000; II, 34,500; III, 23,000; IV, 14,000; V, 12,500; and VI, 9,500. (Although Component V actually consists of two distinct polypeptide species, it will be regarde...

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Cytochrome c oxidase from bakers' yeast. III. Physical characterization of isolated subunits and chemical evidence for two different classes of polypeptides.

Earlier studies have shown that cytochrome c oxidase from bakers' yeast is an oligomeric enzyme which contains three polypeptides (I to III) synthesized on mitochondrial ribosomes and four polypeptides (IV to VII) synthesized on cytoplasmic ribosomes. These polypeptide subunits have now been isolated by a simple protocol which utilizes differences in polypeptide charge, solubility, and size. Th...

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Tissue- and Condition-Specific Isoforms of Mammalian Cytochrome c Oxidase Subunits: From Function to Human Disease

Cytochrome c oxidase (COX) is the terminal enzyme of the electron transport chain and catalyzes the transfer of electrons from cytochrome c to oxygen. COX consists of 14 subunits, three and eleven encoded, respectively, by the mitochondrial and nuclear DNA. Tissue- and condition-specific isoforms have only been reported for COX but not for the other oxidative phosphorylation complexes, suggesti...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1979

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)36010-1