Electrophoretically monodisperse cytochrome c oxidases.
A discontinuous gradient polyacrylamide gel electrophoresis under nondenaturing conditions has been used to demonstrate monodispersity of procaryotic and eucaryotic cytochrome c oxidase preparations. Alkaline treated bovine enzyme which contains nine subunits as analysed by subsequent discontinuous SDS-polyacrylamide gel electrophoresis is a monodisperse dimer in 0.1% Triton X-100 and a monomer in 0.1% dodecyl maltoside. The Mr-values corrected for bound detergent are 286,000 in Triton X-100 and 152,000 in dodecyl maltoside respectively. The two-subunit bacterial cytochrome c oxidase of Paracoccus denitrificans is proved to be a monomer with a corrected Mr of 76,000 in both nonionic detergents Triton X-100 and dodecyl maltoside.
Heinrichs
M
M
Institut für Physikalische Chemie, Abteilung für Biopolymere, RWTH Aachen, FRG.
Buse
G
G
D000818:Animals; D002417:Cattle; D002852:Chromatography, Ion Exchange; D003576:Electron Transport Complex IV / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D009206:Myocardium / Q000201:enzymology*; D010231:Paracoccus denitrificans / Q000201:enzymology*; D010455:Peptides / Q000032:analysis
D010455:Peptides; D003576:Electron Transport Complex IV