Ouabain binding to sodium and potassium dependent adenosine triphosphatase: inhibition by the β,γ methylene analogue of adenosine triphosphate

T. Tobin, T. Akera, R. E. Hogg, T. M. Brody

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

To determine the mechanism of nucleotide dependent, Na+ stimulated binding of [3H]ouabain to (Na+ + K+)-ATPase (EC 3.6.1.3.), we tested the ability of β, γ methylene ATP (adenylylmethylenediphosphonate) to support [3H]ouabain binding. β, γ Methylene ATP is an analogue of AN ANALOGUE OF ATP in which the β and γ phosphates are linked by a methylene group. It is not hydrolyzed by the (Na+ + K+)-ATPase. In the presence of Na+ and Mg++, β, γ methylene ATP did not support [3H]ouabain binding to rat brain (Na+ + K+)-ATPase and it inhibited ATP dependent binding. When [3H]ouabain binding to guinea pig kidney (Na+ + K+)-ATPase was determined in the presence of Na+, Mg++, and Pi, the addition of β, γ methylene ATP was inhibitory, in contrast to the stimulation produced by ATP. The results show that β, γ methylene ATP binds to the (Na+ + K+)-ATPase and that this interaction does not support [3H]ouabain binding.

Original languageEnglish
Pages (from-to)278-281
Number of pages4
JournalMolecular Pharmacology
Volume9
Issue number2
StatePublished - 1973

ASJC Scopus subject areas

  • Molecular Medicine
  • Pharmacology

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