Abstract
Role of supernumerary subunits of bovine heart cytochrome c oxidase has been investigated by examining the influence on the enzymatic activity of their removal by chromatographic procedures or controlled digestion by trypsin. Is has been shown that partial proteolytic cleavage of subunit IV results in depression of respiratory activity and of redox-linked proton translocation. Selective removal by gel-filtration of subunit Vlb has no significant influence on the redox and protonmotive activity of the oxidase.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Cattle
-
Cytochrome a Group
-
Cytochromes / metabolism
-
Electron Transport Complex IV / isolation & purification
-
Electron Transport Complex IV / metabolism*
-
Electrophoresis, Polyacrylamide Gel
-
Kinetics
-
Macromolecular Substances
-
Mitochondria, Heart / enzymology*
-
Peptide Fragments / isolation & purification
-
Trypsin / metabolism
Substances
-
Cytochrome a Group
-
Cytochromes
-
Macromolecular Substances
-
Peptide Fragments
-
Electron Transport Complex IV
-
Trypsin