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

  • Peter Leth Jørgensen


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.


Sulfhydryl Group Tryptophan Fluorescence Ouabain Binding Cytoplasmic Surface Extracellular Surface 
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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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