Hope D B, Wälti M, Winzor D J
Biochem J. 1975 May;147(2):377-9. doi: 10.1042/bj1470377.
The interaction of oxytocin with bovine neurophysin II in 0.1 M-sodium phosphate, pH 5.8, was investigated by equilibrium-dialysis and sedimentation studies. Sigmoidality of the binding curve is attributed to isomerization, either hormone-induced or pre-existing, with preferential binding of oxytocin to one isomeric state. Results are consistent with a binding equation of the form r = (2P[S]+2PQ[S]2)/(1+2P[S]+PQ[S]2) and values of 0.7 X 10(5)M-1 and 1.3 X 10(5)M-1 for P and Q respectively. The significance of these two parameters in relation to current theories of allostery is also discussed.
通过平衡透析和沉降研究，对催产素与牛神经垂体素II在pH 5.8的0.1M磷酸钠溶液中的相互作用进行了研究。结合曲线的S形归因于激素诱导或预先存在的异构化，催产素优先结合到一种异构状态。结果与形式为r = (2P[S]+2PQ[S]2)/(1+2P[S]+PQ[S]2)的结合方程一致，P和Q的值分别为0.7×10(5)M-1和1.3×10(5)M-1。还讨论了这两个参数与当前变构理论的关系。
