Isolation and characterization of cytochrome c oxidase from bird and fish heart mitochondria.
1. Several bird and fish heart mitochondrial cytochrome c oxidases have been isolated with a rapid and simple method involving hydrophobic and affinity chromatography. 2. Their spectrophotometric and kinetic properties are very similar to those of the mammalian enzymes. 3. These oxidases show a polypeptide composition simpler than the mammalian enzymes being composed of 9-10, instead of 13, different polypeptides. 4. These data suggest that the complexity of the mitochondrial heart oxidase increases with the stage of evolution.
Montecucco
C
C
Centro C.N.R. Fisiologia Mitocondri, Università di Padova, Italy.
Schiavo
G
G
Bacci
B
B
Bisson
R
R
D000818:Animals; D001717:Birds / Q000378:metabolism*; D003576:Electron Transport Complex IV / Q000302:isolation & purification* / Q000378:metabolism; D005399:Fishes / Q000378:metabolism*; D007700:Kinetics; D008929:Mitochondria, Heart / Q000201:enzymology*; D013045:Species Specificity
D003576:Electron Transport Complex IV