Abstract
Cytochrome bc1 isolated from Triton X-100-solubilized mitochondrial membranes contains up to 120 nmol of Triton X-100 bound per nanomole of the enzyme. Purified cytochrome bc1 is fully active; however, protein-bound Triton X-100 significantly interferes with structural studies of the enzyme. Removal of Triton X-100 bound to bovine cytochrome bc1 was accomplished by incubation with Bio-Beads SM-2 in the presence of sodium cholate. Sodium cholate is critical because it does not interfere with the adsorption of protein on the hydrophobic surface of the beads. The resulting Triton X-100-free cytochrome bc1 retained nearly full activity, absorption spectra, subunit, and phospholipid composition.
Original language | English (US) |
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Pages (from-to) | 268-270 |
Number of pages | 3 |
Journal | Analytical Biochemistry |
Volume | 395 |
Issue number | 2 |
DOIs | |
State | Published - Dec 15 2009 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology