Isolation of bovine cytochrome c1 as a single non-denatured subunit using gel filtration or high pressure liquid chromatography in deoxycholate
Robinson, N.C.; Talbert, L.
Biochemical and Biophysical Research Communications 95(1): 90-96
1980
ISSN/ISBN: 0006-291X PMID: 6251811 Document Number: 157908
The non-denatured cytochrome c1 subunit of bovine ubiquinone-cytochrome c reductase was isolated using either gel filtration or high pressure liquid chromatography in 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 34.ANG., indicating that the protein either is a dimer in deoxycholate, is asymmetric or binds large amounts of detergent.