Shull G E, Lane L K, Lingrel J B
Nature. 1986;321(6068):429-31. doi: 10.1038/321429a0.
The sodium/potassium-dependent ATPase [(Na+ + K+)ATPase], which establishes and maintains the Na+ and K+ gradients across the plasma membrane of animal cells, consists of two subunits, alpha and beta. Complementary DNA clones encoding the catalytic (alpha) subunit of sheep kidney and Torpedo californica electroplax enzymes have previously been isolated and characterized. However, there is little information concerning the primary structure of the beta-subunit, a glycoprotein of unknown function and relative molecular mass (Mr) approximately 55,000 (ref. 3). Here we describe the isolation and characterization of a cDNA clone containing the entire coding region of the beta-subunit of the sheep kidney (Na+ + K+)ATPase. We also discuss structural aspects of the protein and present evidence for a possible evolutionary relationship with the KdpC subunit of the Escherichia coli K+-ATPase.
钠钾依赖型ATP酶[（Na⁺ + K⁺）ATP酶]负责建立并维持动物细胞质膜两侧的Na⁺和K⁺梯度，它由α和β两个亚基组成。此前已分离并鉴定出编码绵羊肾脏和电鳐电器官酶催化（α）亚基的互补DNA克隆。然而，关于β亚基的一级结构信息却很少，β亚基是一种功能未知、相对分子质量（Mr）约为55,000的糖蛋白（参考文献3）。在此，我们描述了一个包含绵羊肾脏（Na⁺ + K⁺）ATP酶β亚基完整编码区的cDNA克隆的分离与鉴定。我们还讨论了该蛋白质的结构方面，并提供了其与大肠杆菌K⁺-ATP酶的KdpC亚基可能存在进化关系的证据。
