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.
authors.affiliation: Department of Biological Science and Biotechnology, Tsinghua University, Beijing, China.
authors.forename: H P
authors.initials: HP
authors.lastname: Yang
authors.forename: H N
authors.initials: HN
authors.lastname: Zhong
authors.forename: H M
authors.initials: HM
authors.lastname: Zhou
mesh_terms: D000591:Amino Acid Isomerases / Q000378:metabolism*; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D003402:Creatine Kinase / Q000737:chemistry / Q000648:ultrastructure*; D007668:Kidney / Q000201:enzymology; D019696:Peptidylprolyl Isomerase; D011392:Proline / Q000737:chemistry; D011489:Protein Denaturation; D017510:Protein Folding; D013552:Swine
chemical_list: D002352:Carrier Proteins; D011392:Proline; D003402:Creatine Kinase; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase