Isolation of bovine cytochrome c1 as a single non-denatured subunit using gel filtration or high pressure liquid chromatography in deoxycholate

Neal C. Robinson, Linda Talbert

Research output: Contribution to journalArticle

10 Scopus citations


The non-denatured cytochrome c1 subunit of bovine ubiquinone-cytochrome c reductase was isolated using either gel filtration or high pressure liquid chromatography in 1% deoxycholate. The preparation was a single band on polyacrylamide gel electrophoresis in dodecyl sulfate, had a heme content of 31 nmol heme/mg protein, had an absorbance ratio A417/A278 = 2.65, a visible spectrum with maxima at 553, 530, 523.5, 417, 317, and 277 nm for the reduced protein, and an amino acid analysis identical to that previously reported for the isolated denatured protein. The Stokes' radius of this non-denatured deoxycholate solubilized protein was 34Å, indicating that the protein either is a dimer in deoxycholate, is asymmetric, or binds large amounts of detergent.

Original languageEnglish (US)
Pages (from-to)90-96
Number of pages7
JournalTopics in Catalysis
Issue number1
StatePublished - Jan 1 1980


ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Biophysics
  • Molecular Biology

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