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Conformational Changes Associated with K+ Transport by the Na+/K+-ATPase

  • I. M. Glynn
  • S. J. D. Karlish

Abstract

In this article, we discuss two changes of the Na+/K+-ATPase protein: in the first, the phosphorylated enzyme is hydrolyzed and K+ ions bound to the extracellular surface appear to become trapped within; in the second, the trapped K+ ions gain access to the intracellular surface of the enzyme whence they can be released to the cell interior. In each case, the alteration in the accessibility of the K+-binding sites justifies the term conformational change. The interest of these reactions, however, is not that they provide a proper use for an overworked phrase but that there are reasons for believing that the two changes in sequence play a central role in the transport of K+ ions into the cell, which is one of the two primary functions of Na+/K+-ATPase.

Keywords

Intrinsic Fluorescence Extracellular Surface Sodium Medium ATPase Protein Intrinsic Protein Fluorescence 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1982

Authors and Affiliations

  • I. M. Glynn
    • 1
  • S. J. D. Karlish
    • 2
  1. 1.Physiological LaboratoryUniversity of CambridgeCambridgeEngland
  2. 2.Department of BiochemistryWeizmann InstituteRehovothIsrael

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