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  • Title: Exchange between inorganic phosphate and adenosine triphosphate in (Na+,K+)-ATPase.
    Author: Gonçalves de Moraes VL, De Meis L.
    Journal: Biochim Biophys Acta; 1982 May 21; 688(1):131-7. PubMed ID: 6284227.
    Abstract:
    (Na+,K+)-ATPase is able to catalyze a continuous ATP in equilibrium Pi exchange in the presence of Na+ and in the absence of a transmembrane ionic gradient. At pH 7.6 the Na+ concentration required for half-maximal activity is 85 mM and at pH 5.1 it is 340 mM. In the presence of optimal Na+ concentration, the rate of exchange is maximal at pH 6.0 and varies with ADP and Pi concentration in the assay medium. ATP in equilibrium Pi exchange is inhibited by K+ and by ouabain.
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