The uncoupler-induced inactivation of H+-ATPase in liver mitochondria from ground squirrel has been studied. The dependence of this process on Δ81512-M/asset/equation/feb2001457939081512m-math-si1.gif?v=1&s=399d175c88b801e5226466537279d0b3cbca0b92)
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.
