A protein inhibitor of the mitochondrial adenosine triphosphatase complex of rat liver. Purification and characterization.

Nitza Cintron, P. L. Pedersen

Research output: Contribution to journalArticle

80 Citations (Scopus)

Abstract

A heat-stable protein has been purified from rat liver mitochondria which inhibits the ATP hydrolytic activity of both the soluble and membrane-bound mitochondrial F1-ATPase. The overall purification is about 2400-fold with the major purification step consisting of Sephadex "affinity" chromatography. The purified rat liver inhibitor is homogeneous as assessed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis with an apparent molecular weight of 12,300. Amino acid analysis reveals a high content of glutamic acid, lysine, and arginine and the absence of cysteine, proline and methionine. Whether tested with the rat liver or bovine heart ATPase, the liver inhibitor is equally as potent and specific as the heart inhibitor preparation of Pullman and Monroy (Pullman, M.E., and Monroy, G.C. (1963) J. Biol. Chem. 238, 3762-3769). Although the results presented show that the rat liver ATPase inhibitor resembles closely the ATPase inhibitors from other tissues with respect to specific activity and reaction specificity, it is important to note that the rat liver inhibitor is almost 2000 daltons larger than the bovine heart inhibitor, about 5000 daltons larger than ATPase inhibitors of yeast, and contains significantly more lysine residues than both the bovine heart and yeast inhibitors.

Original languageEnglish (US)
Pages (from-to)3439-3443
Number of pages5
JournalJournal of Biological Chemistry
Volume254
Issue number9
StatePublished - May 10 1979
Externally publishedYes

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Proton-Translocating ATPases
Mitochondrial Proteins
Liver
Purification
Rats
Adenosine Triphosphatases
Proteins
Lysine
Yeast
Yeasts
Liver Mitochondrion
Affinity chromatography
Mitochondrial Membranes
Mitochondria
Affinity Chromatography
Proline
Sodium Dodecyl Sulfate
Methionine
Cysteine
Arginine

ASJC Scopus subject areas

  • Biochemistry

Cite this

A protein inhibitor of the mitochondrial adenosine triphosphatase complex of rat liver. Purification and characterization. / Cintron, Nitza; Pedersen, P. L.

In: Journal of Biological Chemistry, Vol. 254, No. 9, 10.05.1979, p. 3439-3443.

Research output: Contribution to journalArticle

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