Literature DB >> 133107

Specific sodium-22 binding to a purified sodium + potassium adenosine triphosphatase. Inhibition by ouabain.

K Kanike, G E Lindenmayer, E T Wallick, L K Lane, A Schwartz.   

Abstract

Analysis of sodium-22 binding to purified sodium + potassium ion-activated adenosine triphosphatase (Na+, K+)-ATPase reveals the presence of two classes of binding sites. The higher affinity site (Kd = 0.2 mM) binds 6 to 7 nmol of sodium per mg of protein. Pretreatment of (Na+, K+)-ATPase with ouabain blocks the binding of sodium to this higher affinity site. Neither heat-denatured enzyme nor phospholipids extracted from the (Na+, K+)-ATPase contain a ouabain-inhibitable, higher affinity sodium binding site. The ouabain enzyme complex therefore appears to contain altered binding sites for cations.

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Year:  1976        PMID: 133107

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  3 in total

1.  Unifying concept for the coupling between ion pumping and ATP hydrolysis or synthesis.

Authors:  G G Hammes
Journal:  Proc Natl Acad Sci U S A       Date:  1982-11       Impact factor: 11.205

2.  The correlation between ouabain binding and potassium pump inhibition in human and sheep erythrocytes.

Authors:  C H Joiner; P K Lauf
Journal:  J Physiol       Date:  1978-10       Impact factor: 5.182

3.  Binding of sodium and potassium to the sodium pump of pig kidney evaluated from nucleotide-binding behaviour.

Authors:  J Jensen; J G Nørby; P Ottolenghi
Journal:  J Physiol       Date:  1984-01       Impact factor: 5.182

  3 in total

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