Comparison of the ATPase activities of bovine heart and liver mitochondrial ATP synthases with different tissue-specific gamma subunit isoforms.
The kinetics of heart and liver mitochondrial ATPase (FoF1) were examined using submitochondrial particles (SMPs) purified from the two tissues to obtain information on the role of gamma subunit isoforms. The F1 portion is mainly composed of the catalytic, common alpha beta subunits and tissue-specific gamma subunits. In contrast to the previous reports on the kinetics and crystallography of various F1's, the Vmax and Km of the two isoforms of FoF1 were identical although the SMPs were prepared from different tissues. Moreover sodium azide inhibited the two equally. The ATPase activity of liver SMP showed slightly steeper pH-dependency than that of heart SMP but the pH optima of the two were the same (pH 8).
Matsuda
C
C
Department of Biochemistry, Jichi Medical School, Tochigi, Japan.
Muneyuki
E
E
Endo
H
H
Yoshida
M
M
Kagawa
Y
Y
D000818:Animals; D001386:Azides / Q000494:pharmacology; D002417:Cattle; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007700:Kinetics; D008929:Mitochondria, Heart / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000201:enzymology*; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D019810:Sodium Azide; D013367:Submitochondrial Particles / Q000201:enzymology; D014018:Tissue Distribution
D001386:Azides; D019810:Sodium Azide; D006180:Proton-Translocating ATPases