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肌酸激酶展开途径中的平衡中间体。

Equilibrium intermediates in the unfolding pathway of creatine kinase.

作者信息

Zhang Y L, Fan Y X, Huang G C, Zhou J X, Zhou J M

机构信息

National Laboratory of Biomacromolecules, Academia Sinica, Beijing, China.

出版信息

Biochem Biophys Res Commun. 1998 May 29;246(3):609-12. doi: 10.1006/bbrc.1998.8673.

DOI:10.1006/bbrc.1998.8673
PMID:9618259
Abstract

The unfolding of creatine kinase in various concentrations of guanidine hydrochloride of increasing concentrations has been investigated by combination of size-exclusion chromatography (SEC) with other methods. There are two peaks in the profiles of SEC in GuHCl at moderate concentrations, showing that unfolding of creatine kinase goes through dimeric and monomeric intermediates with increasing guanidine hydrochloride concentrations. Both intermediates have relatively compact structure and retain considerable ordered structure.

摘要

通过尺寸排阻色谱法(SEC)与其他方法相结合,研究了肌酸激酶在不同浓度递增的盐酸胍中的去折叠情况。在中等浓度的盐酸胍中,SEC图谱出现两个峰,表明随着盐酸胍浓度的增加,肌酸激酶的去折叠过程经历了二聚体和单体中间体阶段。两种中间体都具有相对紧密的结构,并保留了相当程度的有序结构。

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The two slow refolding processes of creatine kinase are catalyzed by cyclophilin.肌酸激酶的两个缓慢重折叠过程由亲环蛋白催化。
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Unfolding and refolding of dimeric creatine kinase equilibrium and kinetic studies.二聚体肌酸激酶的去折叠与重折叠:平衡及动力学研究
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