Sandermann H, Gottwald B A
Biochim Biophys Acta. 1983 Jul 13;732(1):332-5. doi: 10.1016/0005-2736(83)90223-7.
Lipid activation data for (Na+ + K+)-ATPase (Ottolenghi, P. (1979) Eur. J. Biochem. 99, 113-131) have been subjected to a regression and fitting analysis based on a recent kinetic model (Sandermann, H. (1982) Eur. J. Biochem, 127, 123-128). The observed kinetic cooperativity could be generated from strictly non-cooperative binding events involving the known number of 30 boundary lipid-binding sites per ATPase monomer. Apparent lipid dissociation equilibrium constants of between 0.3 and 5 microM were obtained, enzyme activity being associated only with the fully lipid-substituted enzyme and enzyme-lipid complexes with less than six unoccupied lipid-binding sites. The enzyme appeared to operate close to a maximum of cooperativity.
已根据最近的动力学模型（桑德曼，H.（1982年）《欧洲生物化学杂志》，127卷，123 - 128页），对（钠 + 钾）- 三磷酸腺苷酶的脂质激活数据（奥托伦吉，P.（1979年）《欧洲生物化学杂志》，99卷，113 - 131页）进行了回归和拟合分析。观察到的动力学协同性可由涉及每个三磷酸腺苷酶单体已知数量的30个边界脂质结合位点的严格非协同结合事件产生。获得了0.3至5微摩尔之间的表观脂质解离平衡常数，酶活性仅与完全脂质取代的酶以及具有少于六个未占据脂质结合位点的酶 - 脂质复合物相关。该酶似乎在接近最大协同性的状态下运作。
