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Allosteric Interactions with the (Na+ + K+)-dependent Adenosine Triphosphatase

Nature volume 220, pages 1325–1326 (1968)Cite this article

Abstract

Priestland and Whittam1 have questioned the interpretation, in terms of allosteric processes, of certain kinetic studies2,3 of Na+ + K+-dependent adenosine triphosphatase (ATPase). They proposed that competition between Na+ and K+ for the K+-sensitive site on the external surface of the membrane accounts for the sigmoidal effector–velocity curve obtained when one varies the [K+] in the presence of a fixed [Na+], and that this interpretation is an alternative to an allosteric interaction between ions and the enzyme.

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Authors and Affiliations

  1. Department of Pharmacology, State University of New York, Upstate Medical Center, Syracuse, New York

    JOSEPH D. ROBINSON

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  1. JOSEPH D. ROBINSON
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ROBINSON, J. Allosteric Interactions with the (Na+ + K+)-dependent Adenosine Triphosphatase. Nature 220, 1325–1326 (1968). https://doi.org/10.1038/2201325a0

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