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

Hai Peng Yang, Haining Zhong, Hai Meng Zhou

Research output: Contribution to journalArticle

25 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)147-150
Number of pages4
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1338
Issue number2
DOIs
StatePublished - Apr 4 1997
Externally publishedYes

Fingerprint

Peptidylprolyl Isomerase
Creatine Kinase
Catalysis
Urea
Isomerization
Fluorescence
Recovery
Peptides

Keywords

  • Creatine kinase
  • Peptidyl-prolyl isomerase
  • Refolding
  • Urea denaturation

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Structural Biology
  • Biophysics

Cite this

Catalysis of the refolding of urea denatured creatine kinase by peptidyl-prolyl cis-trans isomerase. / Yang, Hai Peng; Zhong, Haining; Zhou, Hai Meng.

In: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, Vol. 1338, No. 2, 04.04.1997, p. 147-150.

Research output: Contribution to journalArticle

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