The effect of the natural protein inhibitor on H+‐ATPase in hepatoma 22a mitochondria

FEBS Letters

Chernyak, B.V.¹  Dukhovich, V.F.¹  Khodjaev, E.Yu.¹ 

[1] A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, Moscow 119899, USSR

关键词: Mitochondria;    ATPase inhibitor protein;    Lubrol-WX disruption;    (Submitochondrial particle;    Hepatoma);    SMP;    submitochondrial particle;    CCCP;    carbonyl cyanide m-chlorophenylhydrazone;    BSA;    bovine serum albumin;   

DOI  :  10.1016/0014-5793(87)80166-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The uncoupler-induced inactivation of H⁺-ATPase in hepatoma 22^a 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.

【 授权许可】

Unknown