The effect of the natural protein inhibitor on H+-ATPase hepatoma 22a mitochondria.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Chernyak BV,Dukhovich VF,Khodjaev EYu

doi

10.1016/0014-5793(87)80166-7

subject

Has Abstract

pub_date

1987-05-11 00:00:00

pages

300-4

issue

2

eissn

0014-5793

issn

1873-3468

journal_volume

215

pub_type

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