Kanike K, Lindenmayer G E, Wallick E T, Lane L K, Schwartz A
J Biol Chem. 1976 Aug 10;251(15):4794-5.
Analysis of sodium-22 binding to purified sodium + potassium ion-activated adenosine triphosphatase (Na+, K+)-ATPase reveals the presence of two classes of binding sites. The higher affinity site (Kd = 0.2 mM) binds 6 to 7 nmol of sodium per mg of protein. Pretreatment of (Na+, K+)-ATPase with ouabain blocks the binding of sodium to this higher affinity site. Neither heat-denatured enzyme nor phospholipids extracted from the (Na+, K+)-ATPase contain a ouabain-inhibitable, higher affinity sodium binding site. The ouabain enzyme complex therefore appears to contain altered binding sites for cations.
对钠-22与纯化的钠钾离子激活的三磷酸腺苷酶(Na⁺,K⁺-ATP酶)结合情况的分析显示存在两类结合位点。高亲和力位点(解离常数Kd = 0.2 mM)每毫克蛋白质结合6至7纳摩尔钠。用哇巴因预处理Na⁺,K⁺-ATP酶可阻断钠与该高亲和力位点的结合。热变性酶和从Na⁺,K⁺-ATP酶中提取的磷脂均不含有可被哇巴因抑制的高亲和力钠结合位点。因此,哇巴因酶复合物似乎含有改变的阳离子结合位点。