Characterization of a Seventh Different Subunit of Beef Heart Cytochrome c Oxidase. Similarities between the Beef Heart Enzyme and That from Other Species

Nancy W. Downer, Neal C. Robinson, Roderick A. Capaldi

Research output: Contribution to journalArticle

176 Scopus citations

Abstract

Beef heart cytochrome c oxidase has been resolved into seven subunits by electrophoresis in highly cross-linked gels containing urea and sodium dodecyl sulfate. The molecular weights of the polypeptides are estimated to be I, 35 400; II, 24 100; III, 21 000; IV, 16 800; V, 12 400; VI, 8200; and VII, 4400. It has been shown that subunits II and III can coelectrophorese on standard sodium dodecyl sulfate-polyacrylamide gels and appear as a single component with an apparent molecular weight of 22 500. This accounts for previous reports that the beef heart enzyme contains only six subunits. Amino acid analysis of the isolated subunits I, II, and III revealed that they have polarities of 35.5, 44.7, and 39.9%, respectively. All three subunits have an extremely high leucine content and a low percentage of basic amino acids relative to subunits IV-VII. The size, number, and properties of subunits in the beef heart cytochrome c oxidase complex suggest that it has essentially the same subunit structure as the complexes isolated from Saccharomyces cerevisiae and Neurospora crassa.

Original languageEnglish (US)
Pages (from-to)2930-2936
Number of pages7
JournalBiochemistry
Volume15
Issue number13
DOIs
StatePublished - Jun 1 1976

ASJC Scopus subject areas

  • Biochemistry

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