钙结合溶菌酶折叠中间体稳定性的比较研究。
Comparative study of the stability of the folding intermediates of the calcium-binding lysozymes.
作者信息
Nitta K, Tsuge H, Iwamoto H
机构信息
Department of Polymer Science, Faculty of Science, Hokkaido University, Japan.
出版信息
Int J Pept Protein Res. 1993 Feb;41(2):118-23. doi: 10.1111/j.1399-3011.1993.tb00121.x.
Unfolding profiles of two calcium-binding lysozymes, equine milk lysozyme and pigeon egg-white lysozyme, were obtained by circular dichroism and proton NMR measurements. Equine lysozyme unfolds through a stable molten globule intermediate. The molten globule of equine lysozyme was characterized as more ordered than that of bovine alpha-lactalbumin. On the other hand, pigeon lysozyme unfolds by a two-state mechanism and the intermediate could not be observed in guanidine or thermal unfolding, the same as with conventional non-calcium-binding lysozymes. Thus, from the point of view of the unfolding profile, equine lysozyme belongs to the group of alpha-lactalbumin, but pigeon lysozyme belongs to the conventional lysozyme group.
通过圆二色性和质子核磁共振测量，获得了两种钙结合溶菌酶（马乳溶菌酶和鸽蛋清溶菌酶）的去折叠谱。马溶菌酶通过稳定的熔融球状体中间体去折叠。马溶菌酶的熔融球状体比牛α-乳白蛋白的熔融球状体更有序。另一方面，鸽溶菌酶通过双态机制去折叠，并且在胍或热去折叠过程中无法观察到中间体，这与传统的非钙结合溶菌酶相同。因此，从去折叠谱的角度来看，马溶菌酶属于α-乳白蛋白组，但鸽溶菌酶属于传统溶菌酶组。
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