Abstract:
: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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Muraguchi M,Yoshihara Y,Tunemitu T,Tani I,Higuti Tdoi
10.1016/0006-291x(90)91697-qsubject
Has Abstractpub_date
1990-04-16 00:00:00pages
226-31issue
1eissn
0006-291Xissn
1090-2104pii
0006-291X(90)91697-Qjournal_volume
168pub_type
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