肽基脯氨酰顺反异构酶催化尿素变性肌酸激酶的复性。

Catalysis of the refolding of urea denatured creatine kinase by peptidyl-prolyl cis-trans isomerase.

作者信息

Yang H P, Zhong H N, Zhou H M

机构信息

Department of Biological Science and Biotechnology, Tsinghua University, Beijing, China.

出版信息

Biochim Biophys Acta. 1997 Apr 4;1338(2):147-50. doi: 10.1016/s0167-4838(97)00026-5.

DOI:10.1016/s0167-4838(97)00026-5

PMID:9128132

Abstract

The effect of peptidyl-prolyl cis-trans isomerase (PPIase) on the refolding and reactivation courses of urea-denatured creatine kinase was followed by fluorescence emission, ultraviolet difference spectra and recovery of activity. PPIase is shown to accelerate the slow-phasic reaction of the refolding of urea-denatured creatine kinase. The results suggest that the prolyl peptide bond isomerization may be one of the rate-determining steps in the refolding of creatine kinase.

摘要

通过荧光发射、紫外差光谱和活性恢复跟踪肽基脯氨酰顺反异构酶（PPIase）对尿素变性肌酸激酶复性和再激活过程的影响。结果表明，PPIase可加速尿素变性肌酸激酶复性的慢相反应。这些结果提示，脯氨酰肽键异构化可能是肌酸激酶复性过程中的限速步骤之一。