Huang G C, Zhou J M
National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.
J Protein Chem. 2000 May;19(4):285-9. doi: 10.1023/a:1007095329303.
A burst phase occurs in the refolding kinetics of guanidine-denatured creatine kinase due to formation of an intermediate within the mixing dead time, with further refolding to the native state after the burst phase along a path following biphasic kinetics. In the presence of cyclophilin, the refolding rates of the two slow processes are accelerated and the values are proportional to the cyclophilin concentration. The activity of cyclophilin in accelerating the slow refolding processes of creatine kinase is totally inhibited by cyclosporin A, indicating that the cis-trans isomerization of the peptidyl-prolyl bonds is involved in the two slow refolding processes.
胍变性肌酸激酶的重折叠动力学中出现一个爆发阶段，这是由于在混合死时间内形成了一种中间体，爆发阶段之后沿着双相动力学路径进一步重折叠至天然状态。在亲环蛋白存在的情况下，两个缓慢过程的重折叠速率加快，且其值与亲环蛋白浓度成正比。亲环蛋白加速肌酸激酶缓慢重折叠过程的活性被环孢菌素A完全抑制，这表明肽基 - 脯氨酰键的顺反异构化参与了这两个缓慢重折叠过程。
