AbstractCross-reconstitution of isolated potato mitochondrial F1-ATPase with F1-depleted beef heart and yeast submitochondrial particles is reported. Potato F1 binds to the heterologous membrane and confers oligomycin sensitivity on the ATPase activity of the reconstituted system. Binding of F1 is promoted by the presence of Mg2+ with the maximal stimulatory efrect at 20 mM. Mg2+ increase the sensitivity to oligomycin of the reconstituted system consisting of potato F1 and yeast membranes, however, they do not influence oligomycin sensitivity of potato F1 and beef heart membranes
In order to assess the role of thiol groups in the Fo part of the ATP synthase in the coupling mecha...
The mitochondrial F-ATPase can be activated either by the classical cofactor Mg2+ or, with lower eff...
The inner mitochondrial membrane is selectively permeable, which limits the transport of solutes and...
AbstractCross-reconstitution of isolated potato mitochondrial F1-ATPase with F1-depleted beef heart ...
AbstractThe ATP-hydrolyzing activity of F1-ATPase purified from potato tubers mitochondria was stimu...
AbstractThe effect of some F0F1 inhibitors on the activation of the H+-ATPase by the electrochemical...
1. An oligomycin -sensitive ATPase was isolated and partially purified from beef heart mitochondria....
1. To have a rapid isolation of oligomycin-sensitive ATPase particles (OSA particles), 0.1 mg DOC pe...
AbstractSoluble beef-heart mitochondrial F1-ATPase modified in its α-subunit by mild trypsin treatme...
AbstractThe membrane F0, sector of mitochondrial ATP synthase complex was rapidly isolated by direct...
Recent results suggest that the mitochondrial permeability transition pore (PTP) in mammals is actua...
AbstractMild trypsin digestion of isolated bovine-heart mitochondrial F1-ATPase removed the first 15...
AbstractThe binding parameters of the oligomycin-sensitivity conferring protein (OSCP) in inside-out...
In animal cells Ca2+ and ROS induce a sudden change in the inner mitochondrial membrane permeability...
The mechanism of beef heart mitochondrial ATPase (F(,1)) was studied using chromium (III) substitute...
In order to assess the role of thiol groups in the Fo part of the ATP synthase in the coupling mecha...
The mitochondrial F-ATPase can be activated either by the classical cofactor Mg2+ or, with lower eff...
The inner mitochondrial membrane is selectively permeable, which limits the transport of solutes and...
AbstractCross-reconstitution of isolated potato mitochondrial F1-ATPase with F1-depleted beef heart ...
AbstractThe ATP-hydrolyzing activity of F1-ATPase purified from potato tubers mitochondria was stimu...
AbstractThe effect of some F0F1 inhibitors on the activation of the H+-ATPase by the electrochemical...
1. An oligomycin -sensitive ATPase was isolated and partially purified from beef heart mitochondria....
1. To have a rapid isolation of oligomycin-sensitive ATPase particles (OSA particles), 0.1 mg DOC pe...
AbstractSoluble beef-heart mitochondrial F1-ATPase modified in its α-subunit by mild trypsin treatme...
AbstractThe membrane F0, sector of mitochondrial ATP synthase complex was rapidly isolated by direct...
Recent results suggest that the mitochondrial permeability transition pore (PTP) in mammals is actua...
AbstractMild trypsin digestion of isolated bovine-heart mitochondrial F1-ATPase removed the first 15...
AbstractThe binding parameters of the oligomycin-sensitivity conferring protein (OSCP) in inside-out...
In animal cells Ca2+ and ROS induce a sudden change in the inner mitochondrial membrane permeability...
The mechanism of beef heart mitochondrial ATPase (F(,1)) was studied using chromium (III) substitute...
In order to assess the role of thiol groups in the Fo part of the ATP synthase in the coupling mecha...
The mitochondrial F-ATPase can be activated either by the classical cofactor Mg2+ or, with lower eff...
The inner mitochondrial membrane is selectively permeable, which limits the transport of solutes and...