Removal of bound Triton X-100 from purified bovine heart cytochrome bc1

Rastislav Varhač, Neal C. Robinson, Andrej Musatov

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

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 languageEnglish (US)
Pages (from-to)268-270
Number of pages3
JournalAnalytical Biochemistry
Volume395
Issue number2
DOIs
StatePublished - Dec 15 2009

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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