Purification of an ATPase Inhibitor Peptide Fraction from Rat Liver Mitochondria

Nitza M. Cintrón, Peter L. Pedersen

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

This chapter describes an inhibitor peptide of the mitochondrial ATPase from beef heart. It discusses the suppression of the hydrolytic activity of purified and membrane-bound F1 ATPase. It has been suggested that the function of this inhibitor is that of a vectorial regulator in respiratory-chain-linked energy transfers. The chapter indentifies a trypsin-sensitive inhibitor activity in the rat liver mitochondrial system and describes the procedure for its purification. It describes analytical procedures, which include measurement and ATPase inhibitor activity and measurement of protein. It also discusses purification procedures, which includes isolation of mitochondria, alkaline extraction, ammonium sulfate precipitation, trichloroacetic acid precipitation, concentration by Sephadex solvent absorption, heat treatment, and Sephadex G-75 gel filtration affinity chromatography. The chapter provides an overview on the general properties of the inhibitor protein fraction. It examines the differences among the various inhibitors.

Original languageEnglish (US)
Pages (from-to)408-414
Number of pages7
JournalMethods in enzymology
Volume55
Issue numberC
DOIs
StatePublished - Jan 1 1979
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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