Discrimination between the binding sites of modulators of the H+-translocating ATPase activity in rat liver mitochondrial membranes.
The properties of the components of the mitochondrial ATPase which interact with modulators of energy transduction have been examined. The chromatographic behavior and the size of the components which bind trialkyl tins, carbodiimides and uncouplers, have been shown to be different. However, they all appear to be proteolipids with apparent molecular weights around 10,000. On this basis it is proposed that these inhibitors act at different sites in the membrane sector of the ATP synthase of rat liver mitochondria.
D000818:Animals; D001665:Binding Sites; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone / Q000031:analogs & derivatives / Q000378:metabolism; D004024:Dicyclohexylcarbodiimide / Q000378:metabolism; D066298:In Vitro Techniques; D007425:Intracellular Membranes / Q000201:enzymology; D008930:Mitochondria, Liver / Q000201:enzymology*; D009570:Nitriles / Q000378:metabolism; D011485:Protein Binding; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D051381:Rats; D013367:Submitochondrial Particles / Q000201:enzymology; D014220:Trialkyltin Compounds / Q000378:metabolism; D014475:Uncoupling Agents / Q000378:metabolism
C042050:4-azido-2-nitrocarbonylocyanide phenyl hydrazone; D009570:Nitriles; D014220:Trialkyltin Compounds; D014475:Uncoupling Agents; D004024:Dicyclohexylcarbodiimide; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone; C015129:dibutylchloro(chloromethyl)tin; D006180:Proton-Translocating ATPases