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The localization of tightly bound cardiolipin in cytochrome oxidase.

Authors
  • Fry, M
  • Blondin, G A
  • Green, D E
Type
Published Article
Journal
Journal of Biological Chemistry
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Publication Date
Oct 25, 1980
Volume
255
Issue
20
Pages
9967–9970
Identifiers
PMID: 6253460
Source
Medline
License
Unknown

Abstract

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.

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