The localization of tightly bound cardiolipin in cytochrome oxidase.
One to two molecules of tightly bound cardiolipin are associated with resolved fractions of cytochrome oxidase containing subunits I to III or I to IV. Large scale isolation of subunits I to IV indicates the presence of approximately 0.5 molecule of cardiolipin per molecule of subunit I. Lipoprotein staining of sodium dodecyl sulfate/urea/acrylamide gels of cytochrome oxidase support the findings that subunit I is a lipoprotein. The resistance of this tightly bound cardiolipin to organic solvent extraction suggests a specific association of some tenacity with the protein.
D001665:Binding Sites; D002308:Cardiolipins / Q000032:analysis*; D003576:Electron Transport Complex IV / Q000032:analysis*; D046911:Macromolecular Substances; D010743:Phospholipids / Q000032:analysis; D011485:Protein Binding
D002308:Cardiolipins; D046911:Macromolecular Substances; D010743:Phospholipids; D003576:Electron Transport Complex IV