This paper, reviews recent findings on the protein components of the Na
+ pump, the protein-phospholipid interactions, the reaction sequence of Na
+, K
+-ATPase, the transport mode of Na
+ pump, the binding of physiological ligands to Na
+, K
+-ATPase, the relation between partial reactions and various phosphoenzymes and the conformational changes of Na
+, K
+-ATPase. Available data show that these phosphoenzymes are reaction intermediates in not only the hydrolysis of ATP but also the transport of Na
+ and K
+ across the membrane. Recent findings on the conformational change of Na
+, K
+-ATPase detected by intrinsic and extrinsic protein probes suggest that the free energy generated by ATP hydrolysis is converted to conformational energy during the conversion of MgNaE
1P to MgE
2P.
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