Foussard-Guilbert F, Ermias A, Laget P, Tanguy G, Girault M, Jallet P
Biochim Biophys Acta. 1982 Nov 8;692(2):296-304. doi: 10.1016/0005-2736(82)90534-x.
Studies on (Na+ +K+)-ATPase generally employ detergents such as SDS and deoxycholate. Under such conditions, the purified enzyme possesses high specific activity. The (Na+ +K+)-ATPase from kidney membranes was unmasked by deoxycholate and SDS as described by Jłrgensen and its kinetic properties were studied. The results suggest that these detergents induce some irreversible alterations in the kinetic properties of the native enzyme. Another detergent, saponin, unmasked the (Na+ +K+)-ATPase as effectively as did SDS, but it seems to affect the kinetic properties of the native enzyme to a lesser extent.
对（钠+钾）-ATP酶的研究通常使用十二烷基硫酸钠（SDS）和脱氧胆酸盐等去污剂。在这种条件下，纯化后的酶具有较高的比活性。如约根森所述，脱氧胆酸盐和SDS可使肾膜中的（钠+钾）-ATP酶暴露出来，并对其动力学特性进行了研究。结果表明，这些去污剂会使天然酶的动力学特性发生一些不可逆的改变。另一种去污剂皂角苷，与SDS一样有效地使（钠+钾）-ATP酶暴露出来，但它对天然酶动力学特性的影响似乎较小。
