Isolation of bovine cytochrome c1 as a single non-denatured subunit using gel filtration or high pressure liquid chromatography in deoxycholate |
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Authors: | N C Robinson L Talbert |
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Institution: | Department of Biochemistry, The University of Texas Health Science Center at San Antonio, San Antonio, Texas 78284 USA |
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Abstract: | The non-denatured cytochrome subunit of bovine ubiquinone-cytochrome 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 , 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. |
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Keywords: | To whom correspondence should be addressed |
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