Michael L, Wallick E T, Schwartz A
J Biol Chem. 1977 Dec 10;252(23):8476-80.
Antibodies (abys) raised to (Na+,K+)-ATPase were purified by elution methods and shown to be cross-reactive with anti-gamma-globulin and the original antigen. Abys were isolated from two different antisera and the effects on (Na+,K+)-ATPase hydrolytic activity and [3H]ouabain binding were measured. The antisera fractions differed as to their maximum level of inhibition of hydrolytic activity and maximal [3H]ouabain binding, but both fractions caused inhibition of maximal [3H]ouabain binding to the same quantitative extent as inhibition of hydrolytic activity. Variable effects on the rate of [3H]ouabain binding were noted which were highly dependent on ligand conditions. During the "turnover state conditions" of the enzyme, the abys stimulated the rate of [3H]ouabain binding to the (Na+,K+)-ATPase. We conclude that effects of aby-(Na+,K+)-ATPase interaction depend upon degree of purity of aby, specificity, aby/enzyme ratios, and ligand conditions.
通过洗脱方法纯化了针对（钠钾）-ATP酶产生的抗体，并证明其与抗γ球蛋白和原始抗原具有交叉反应性。从两种不同的抗血清中分离出抗体，并测量其对（钠钾）-ATP酶水解活性和[3H]哇巴因结合的影响。抗血清组分在水解活性的最大抑制水平和最大[3H]哇巴因结合方面存在差异，但两个组分对最大[3H]哇巴因结合的抑制程度与水解活性的抑制程度在数量上相同。观察到对[3H]哇巴因结合速率的可变影响，这高度依赖于配体条件。在酶的“周转状态条件”下，抗体刺激了[3H]哇巴因与（钠钾）-ATP酶的结合速率。我们得出结论，抗体-（钠钾）-ATP酶相互作用的影响取决于抗体的纯度、特异性、抗体/酶比例和配体条件。
