Spectroscopic determination of cytochrome c oxidase content in tissues containing myoglobin or hemoglobin

Anal Biochem. 1996 Jun 1;237(2):274-8. doi: 10.1006/abio.1996.0239.

Abstract

A simple spectroscopic method for determining the cytochrome c oxidase, cytochrome a, a3, content in tissue and mitochondria samples independent of myoglobin or blood contamination is described. Using tissue homogenates solubilized in Triton X-100, this assay relies on the selective reduction of mitochondrial cytochromes by the action of potassium cyanide. Monitoring the optical absorbance of these samples at 605 nm provided a quantitative determination of cytochrome c oxidase content in the presence of myoglobin or blood. The cytochrome c oxidase content of porcine heart mitochondria and whole tissue was determined to be 0.85 nmol/mg protein and 30.5 nmol/g wet wt, respectively.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Detergents
  • Electron Transport Complex IV / analysis*
  • Evaluation Studies as Topic
  • Hemoglobins / analysis*
  • Mitochondria, Heart / chemistry
  • Myocardium / chemistry
  • Myoglobin / analysis*
  • Octoxynol
  • Potassium Cyanide
  • Spectrophotometry / methods*
  • Swine

Substances

  • Detergents
  • Hemoglobins
  • Myoglobin
  • Octoxynol
  • Electron Transport Complex IV
  • Potassium Cyanide