Allosteric interactions with the (na+ + k+)-dependent adenosine triphosphatase

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. Access through your institution Buy

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ANALYSIS OF COOPERATIVE LIGAND BINDING BY THE ATP-BINDING DNA APTAMER INDICATES A POPULATION-SHIFT BINDING MECHANISM Article Open access 03 November 2020 REFERENCES * Priestland, R. N., and

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references AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Department of Pharmacology, State University of New York, Upstate Medical Center, Syracuse, New York JOSEPH D. ROBINSON Authors *

JOSEPH D. ROBINSON View author publications You can also search for this author inPubMed Google Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE

ROBINSON, J. Allosteric Interactions with the (Na+ + K+)-dependent Adenosine Triphosphatase. _Nature_ 220, 1325–1326 (1968). https://doi.org/10.1038/2201325a0 Download citation * Received:

25 October 1968 * Issue Date: 28 December 1968 * DOI: https://doi.org/10.1038/2201325a0 SHARE THIS ARTICLE Anyone you share the following link with will be able to read this content: Get

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