The effect of the natural protein inhibitor on H+‐ATPase in hepatoma 22a mitochondria
- 11 May 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 215 (2) , 300-304
- https://doi.org/10.1016/0014-5793(87)80166-7
Abstract
The uncoupler-induced inactivation of H+-ATPase in hepatoma 22a and mouse liver mitochondria has been studied. The dependence of this process on ΔμH, and pH and ATP was established. The inactivated ATPase could be reactivated at alkaline pH values in the absence of ATP. These data indicate that the inactivation is apparently caused by the natural protein inhibitor. ATP- and pH-dependent decrease of ATPase activity is also observed after Lubrol-WX disruption of mitochondria. It can be proposed that practically all ATPase molecules in hepatoma mitochondria are in a catalytically active complex with the protein inhibitor. At low ΔμH this complex is inactivated via reversible pH-dependent and irreversible ATP-dependent rearrangements. The pH-dependent rearrangement of the isolated protein inhibitor from hepatoma mitrochondria is also observed.Keywords
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