Purification of α and β subunits and subunit pairs from rat liver mitochondrial F1-ATPase

Noreen Williams, Peter L. Pedersen

Research output: Contribution to journalArticlepeer-review

Abstract

This chapter describes a procedure for the purification of α and β subunits and subunit pairs from rat liver mitochondrial F1-ATPase. The procedure for separation based on cold treatment with subsequent purification is described. The protocols combining cold treatment for dissociation of the rat liver mitochondrial F1-ATPase together with chromatographic separation allow the purification of the two major subunits, α and β, and two subunit complexes, αγ and βγ. The complexes are both stable to treatment and are not affected by the presence of dithiothreitol during cold treatment or purification. Neither the individual subunits (α and β) nor the subunit complexes (αγ and βγ) are capable of catalysis. However, under the appropriate conditions (the addition of Mg2+ and ATP), the supernatant and sediment fractions reconstitute to yield 100% of the control activity, indicating that they are still competent.

Original languageEnglish (US)
Pages (from-to)484-489
Number of pages6
JournalMethods in enzymology
Volume126
Issue numberC
DOIs
StatePublished - Jan 1 1986

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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