Pearlmutter A F, Dalton E J
Int J Pept Protein Res. 1980 Nov;16(5):477-81. doi: 10.1111/j.1399-3011.1980.tb02972.x.
By use of stopped-flow kinetic data, we have measured the kinetics of mononitrated neurophysin I monomer binding to oxytocin. The association constant was 1.3(+/-0.3) x 10(5) M-1s-1 and the dissociation rate constant was 2.0(+/-0.5)s-1 for protonated oxytocin binding. Both rates are significantly slower than those observed for neurophysin dimer. These data suggest that the binding process by which the monomer binds oxytocin is not identical to that of dimer.
通过使用停流动力学数据，我们测量了单硝化神经垂体素I单体与催产素结合的动力学。对于质子化催产素结合，缔合常数为1.3（±0.3）×10⁵ M⁻¹s⁻¹，解离速率常数为2.0（±0.5）s⁻¹。这两个速率都明显慢于神经垂体素二聚体所观察到的速率。这些数据表明，单体结合催产素的结合过程与二聚体的不同。
