Na⁺ポンプのメカニズム

抄録

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 MgNaE₁P to MgE₂P.