Catalysis of the refolding of urea denatured creatine kinase by peptidyl-prolyl cis-trans isomerase.
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.
Yang
H P
HP
Department of Biological Science and Biotechnology, Tsinghua University, Beijing, China.
Zhong
H N
HN
Zhou
H M
HM
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
D002352:Carrier Proteins; D011392:Proline; D003402:Creatine Kinase; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase