Regulation of ATP hydrolysis in liver mitochondria from ground squirrel
- 18 June 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 266 (1-2) , 83-86
- https://doi.org/10.1016/0014-5793(90)81512-m
Abstract
The uncoupler‐induced inactivation of H+‐ATPase in liver mitochondria from ground squirrel has been studied. The dependence of this process on Δ gmH+, pH and ATP indicates that it is caused by the protein inhibitor. This conclusion is also supported by the protective effect of Zn2+ and Cu2+. The inactivation can be induced by Ca2+ at low concentrations in the presence of phosphate. It is shown that the protein inhibitor inactivates ATPase almost completely under optimal conditions while its effect in mice or rat liver mitochondria does not exceed 30%. The potential efficiency of the inhibitor's action does not depend on either the season or the state of animals (hibernating or active). At the same time, the sensitivity of this system to Ca2+ is significantly lower in active (summer) animals.Keywords
This publication has 6 references indexed in Scilit:
- The effect of the natural protein inhibitor on H+‐ATPase in hepatoma 22a mitochondriaFEBS Letters, 1987
- Regulation of the mitochondrial ATP synthase/ATPase complexArchives of Biochemistry and Biophysics, 1986
- Regulation of H+-ATPases in oxidative- and photophosphorylationTrends in Biochemical Sciences, 1986
- The oxidation of sulfhydryl groups in mitochondrial F1‐ATPase decreases the rate of its inactivation by the natural protein inhibitorFEBS Letters, 1985
- Interaction between the mitochondrial ATP synthetase and ATPase inhibitor proteinFEBS Letters, 1985
- A Naturally Occurring Inhibitor of Mitochondrial Adenosine TriphosphataseJournal of Biological Chemistry, 1963