Kometiani Z P, Vekua M G
Biokhimiia. 1983 Jun;48(6):1025-30.
An analysis of the shapes of the kinetic curves for the cationic sites of the Na,K-ATPase system revealed four completely activated Na-sites. Free ATP can change the so-called operation regime of Na,K-ATPase. At ATP excess two completely activated K-sites are detected, whereas at low ATP concentrations only one incompletely activated site is observed.
对钠钾ATP酶系统阳离子位点动力学曲线形状的分析揭示了四个完全激活的钠位点。游离ATP可以改变钠钾ATP酶的所谓运转模式。在ATP过量时，检测到两个完全激活的钾位点，而在低ATP浓度下，仅观察到一个未完全激活的位点。
