Isolation and properties of OSCP and an F1-ATPase binding protein from rat liver mitochondria - Evidence against OSCP as the linking "stalk" between F1 and the membrane

Leland K. Russell, Scott A. Kirkley, Thomas R. Kleyman, Samuel H.P. Chan

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19 Scopus citations


Oligomycin Sensitivity Conferral Protein (OSCP) and an F1-ATPase Binding Protein were isolated from F1-depleted rat liver mitochondrial membrane. Their molecular weights on polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and urea were 22,500 and 8,500 respectively. When incubated with liver TUA (trypsin, urea and ammonia-treated) submitochondrial particles, the binding protein was effective in the binding of F1 to the particles with the resultant particle-bound ATPase activity not oligomycin sensitive. When OSCP was then incubated with the reconstituted membrane-bound ATPase, its activity became oligomycin sensitive. These results suggest that, first; the binding protein, but not OSCP, connects F1-ATPase to the membrane of rat liver mitochondria and maybe to the "stalk", if indeed there is a stalk in mitochondrial membrane ATPase complex; and second; the function of OSCP is solely to render the ATPase activity sensitive to oligomycin and other similar inhibitors.

Original languageEnglish (US)
Pages (from-to)434-443
Number of pages10
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Nov 22 1976

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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