Hawley S A, Mitchell R M
Biochemistry. 1975 Jul 15;14(14):3257-64. doi: 10.1021/bi00685a036.
When reversible denaturation of chymotrypsinogen is produced at elevated hydrostatic pressures, conformational relaxation can occur quite slowly, allowing electrophoretic separation of the principal states from the equilibrium mixture. In this work we report experimental concentration distribution patterns obtained at pH 2.03 at a temperature of 20.5 degrees and find them to be reasonably consistent with the behavior that is expected from a simple two-state isomerism. However, the results do not at all rule out the existence of low levels of intermediate states.
当在升高的流体静压力下产生胰凝乳蛋白酶原的可逆变性时，构象弛豫可能会相当缓慢地发生，从而允许从平衡混合物中对主要状态进行电泳分离。在这项工作中，我们报告了在20.5摄氏度、pH值为2.03时获得的实验浓度分布模式，并发现它们与简单二态异构所预期的行为相当一致。然而，这些结果丝毫没有排除低水平中间状态的存在。
