Purification and properties of ATPase inhibitor from rat liver mitochondria

Samuel H.P. Chan, Randall L. Barbour

Research output: Contribution to journalArticle

47 Scopus citations

Abstract

(1) The ATPase inhibitor protein has been isolated from rat liver mitochondria in purified form. The molecular weight determined by sodium dodecyl sulfate gel electrophoresis is approximately 9500, and the isoelectric point is 8.9. (2) The protein inhibits both the soluble ATPase and the particle-bound ATPase from rat liver mitochondria. It also inhibits ATPase activities of soluble F1, and inhibitor-depleted submitochondrial particles derived from bovine heart mitochondria. (3) On particle-bound ATPase the inhibitor has its maximal effect if incubated in the presence of Mg2+. ATP at slightly acidic pH. (4) The inhibitor has a minimal effect on Pi-ATP exchange activity in sonicated submitochondrial particles. However, unexpectedly the inhibitor greatly stimulates Pi-ATP exchange activity in whole mitochondria while the low ATPase activity of the mitochondria is not affected. The possible mechanism of action of the inhibitor on intact mitochondria is offered.

Original languageEnglish (US)
Pages (from-to)426-433
Number of pages8
JournalBBA - Bioenergetics
Volume430
Issue number3
DOIs
StatePublished - Jun 8 1976

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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