Stoichiometry of chargerin II (A6L) in the H(+)-ATP synthase of rat liver mitochondria.
Previous studies suggested that the hydrophobic protein chargerin II, which is encoded in the A6L of mitochondrial DNA, may have a key role in the energy transduction by mitochondrial H(+)-ATP synthase because an antibody against chargerin II inhibited ATP synthesis and ATP-Pi exchange, in an energy-dependent fashion. In the present work, the contents of chargerin II in the H(+)-ATP synthase purified from rat liver mitochondria and in submitochondrial particles were determined by radioimmunoassay. Results showed that the H(+)-ATP synthase contained chargerin II in a molar ratio of one to one. This is the first report on the stoichiometry of the A6L-product in mitochondrial H(+)-ATP synthase.
Muraguchi
M
M
Faculty of Pharmaceutical Sciences, University of Tokushima, Japan.
Yoshihara
Y
Y
Tunemitu
T
T
Tani
I
I
Higuti
T
T
D000818:Animals; D015153:Blotting, Western; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000032:analysis* / Q000648:ultrastructure; D008930:Mitochondria, Liver / Q000201:enzymology*; D006180:Proton-Translocating ATPases / Q000032:analysis*; D011863:Radioimmunoassay; D051381:Rats; D013367:Submitochondrial Particles / Q000032:analysis
D046911:Macromolecular Substances; D008565:Membrane Proteins; C044593:chargerins; D006180:Proton-Translocating ATPases