An active cytochrome c oxidase that has no tightly bound cardiolipin
- 1 March 1983
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 209 (3) , 901-903
- https://doi.org/10.1042/bj2090901
Abstract
Bovine and dogfish (Squalus acanthias) heart submitochondrial particles and cytochrome c oxidase (EC 1.9.3.1) were prepared. Biphasic Eadie-Hofstee plots from steady-state polarographic assays were obtained for both species. Phospholipid analyses indicated that cardiolipin was absent from this active dogfish enzyme.This publication has 11 references indexed in Scilit:
- Specificity and binding affinity of phospholipids to the high-affinity cardiolipin sites of beef heart cytochrome c oxidaseBiochemistry, 1982
- Diphosphatidylglycerol is required for optimal activity of beef heart cytochrome c oxidase.Proceedings of the National Academy of Sciences, 1981
- Structural and functional properties of cytochrome c oxidases isolated from sharks.Journal of Biological Chemistry, 1980
- Lipid-substituted cytochrome oxidase: No absolute requirement of cardiolipin for activityBiochemical and Biophysical Research Communications, 1978
- Definition of cytochrome c binding domains by chemical modification. III. Kinetics of reaction of carboxydinitrophenyl cytochromes c with cytochrome c oxidase.Journal of Biological Chemistry, 1978
- Components of the mitochondrial inner membrane. 5. Interaction of detergents with cytochrome c oxidaseBiochemistry, 1977
- Correlation of the kinetics of electron transfer activity of various eukaryotic cytochromes c with binding to mitochondrial cytochrome c oxidase.Journal of Biological Chemistry, 1976
- A RAPID METHOD OF TOTAL LIPID EXTRACTION AND PURIFICATIONCanadian Journal of Biochemistry and Physiology, 1959