oligomycins has been researched along with potassium-phosphate* in 1 studies
1 other study(ies) available for oligomycins and potassium-phosphate
| Article | Year |
|---|---|
Flux-dependent increase in the stoichiometry of charge translocation by mitochondrial ATPase/ATP synthase induced by almitrine.
After studying the effects of almitrine, a new kind of ATPase/ATP synthase inhibitor, on two kinds of isolated mammalian mitochondrion, we have observed that: (1) Almitrine inhibits oligomycin-sensitive ATPase; it decreases the ATP/O value of oxidative phosphorylations without any change in the magnitude of delta mu H+. (2) Almitrine increases the mechanistic H+/ATP stoichiometry of ATPase as shown by measuring either (i) the extent of potassium acetate and of potassium phosphate accumulation sustained by ATP utilisation, or (ii) the electrical charge/ATP (K+/ATP) ratio at steady-state of ATPase activity. (3) Rat liver mitochondria are at least 10-times more sensitive to almitrine than beef heart mitochondria. (4) The change in H+/ATP stoichiometry induced by almitrine depends on the magnitude of the flux through ATPase. The inhibitory effect of almitrine on ATPase/ATP synthase complex, as a consequence of such an H+/ATP stoichiometry change, is discussed. Topics: Acetates; Acetic Acid; Adenosine Triphosphatases; Adenosine Triphosphate; Almitrine; Animals; Cattle; Male; Mitochondria, Heart; Mitochondria, Liver; Mitochondrial Swelling; Oligomycins; Oxidative Phosphorylation; Phosphates; Potassium; Potassium Compounds; Proton-Translocating ATPases; Protons; Rats; Rats, Inbred Strains; Valinomycin | 1990 |