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

Hai Peng Yang; Hai Ning Zhong; Hai Meng Zhou

doi:10.1016/S0167-4838(97)00026-5

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

Hai Peng Yang, Hai Ning Zhong, Hai Meng Zhou

Research output: Contribution to journal › Article › peer-review

25 Scopus citations

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.

Original language	English (US)
Pages (from-to)	147-150
Number of pages	4
Journal	Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume	1338
Issue number	2
DOIs	https://doi.org/10.1016/S0167-4838(97)00026-5
State	Published - Apr 4 1997
Externally published	Yes

Keywords

Creatine kinase
Peptidyl-prolyl isomerase
Refolding
Urea denaturation

ASJC Scopus subject areas

Molecular Biology
Structural Biology
Biophysics
Biochemistry

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10.1016/S0167-4838(97)00026-5

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title = "Catalysis of the refolding of urea denatured creatine kinase by peptidyl-prolyl cis-trans isomerase",

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.",

keywords = "Creatine kinase, Peptidyl-prolyl isomerase, Refolding, Urea denaturation",

author = "Yang, {Hai Peng} and Zhong, {Hai Ning} and Zhou, {Hai Meng}",

note = "Funding Information: The present investigation was supported in part by the Pandeng Project of the China Commission for Science and Technology and by Grant 39570180 of the China Natural Science Foundation.",

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T1 - Catalysis of the refolding of urea denatured creatine kinase by peptidyl-prolyl cis-trans isomerase

AU - Yang, Hai Peng

AU - Zhong, Hai Ning

AU - Zhou, Hai Meng

N1 - Funding Information: The present investigation was supported in part by the Pandeng Project of the China Commission for Science and Technology and by Grant 39570180 of the China Natural Science Foundation.

PY - 1997/4/4

Y1 - 1997/4/4

N2 - 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.

AB - 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.

KW - Creatine kinase

KW - Peptidyl-prolyl isomerase

KW - Refolding

KW - Urea denaturation

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

Abstract

Keywords

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