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Topology in the Membrane and Principal Conformations of the α Subunit of Na+/K+- ATPase

  • Peter Leth Jørgensen

Abstract

A significant gap in our understanding of the reaction mechanism of the Na+/K+ pump is the lack of information about the molecular structure of the protein. Pure preparations of the proteins of Na+/K+-ATPase have been available for a decade, but analysis of the primary structure is complicated by aggregation of hydrophobic segments and the three-dimensional structure is unknown. Some provisional information is available about the organization of the protein in the membrane (Jørgensen, 1977; Karlish et al., 1977; Castro and Farley, 1979). In addition, controlled proteolysis of the α subunit (Jørgensen, 1975, 1977; Giotta, 1975) and fluorescence analysis (Karlish and Yates, 1978; Jørgensen and Karlish, 1980; Karlish, 1980; Hegyvary and Jørgensen, 1981) show that the protein can assume two principal conformations.

Keywords

Sulfhydryl Group Tryptophan Fluorescence Ouabain Binding Cytoplasmic Surface Extracellular Surface 
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

  • Peter Leth Jørgensen
    • 1
  1. 1.Institute of PhysiologyUniversity of AarhusAarhus CDenmark

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