Chernyak B V, Dukhovich V F
FEBS Lett. 1987 May 11;215(2):300-4. doi: 10.1016/0014-5793(87)80166-7.
The uncoupler-induced inactivation of H+-ATPase in hepatoma 22a and mouse liver mitochondria has been studied. The dependence of this process on delta microH, 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 delta microH this complex is inactivated via reversible pH-dependent and irreversible ATP-dependent rearrangements. The pH-dependent rearrangement of the isolated protein inhibitor from hepatoma mitochondria is also observed.
对解偶联剂诱导肝癌22a和小鼠肝脏线粒体中H⁺-ATP酶失活的情况进行了研究。确定了该过程对ΔμH、pH值和ATP的依赖性。失活的ATP酶在无ATP的碱性pH值条件下可重新激活。这些数据表明，失活显然是由天然蛋白质抑制剂引起的。用Lubrol-WX破坏线粒体后，也观察到ATP酶活性依赖于ATP和pH值的降低。可以推测，肝癌线粒体中几乎所有的ATP酶分子都与蛋白质抑制剂形成了具有催化活性的复合物。在低ΔμH时，该复合物通过可逆的pH依赖性和不可逆的ATP依赖性重排而失活。还观察到来自肝癌线粒体的分离蛋白质抑制剂的pH依赖性重排。
