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Discrimination between the binding sites of modulators of the H+-translocating ATPase activity in rat liver mitochondrial membranes

Authors
Journal
Archives of Biochemistry and Biophysics
0003-9861
Publisher
Elsevier
Publication Date
Volume
232
Issue
2
Identifiers
DOI: 10.1016/0003-9861(84)90580-0
Keywords
  • Biological Oxidations And Bioenergetics

Abstract

Abstract The properties of the components of the mitochondrial ATPase which interact with modulators of energy transduction have been examined. The chromatographic behavior and the size of the components which bind trialkyl tins, carbodiimides and uncouplers, have been shown to be different. However, they all appear to be proteolipids with apparent molecular weights around 10,000. On this basis it is proposed that these inhibitors act at different sites in the membrane sector of the ATP synthase of rat liver mitochondria.

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