Answers are grounded in this paper and cite their sources.
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.
No takes yet. Share an insight, caveat, or question.
Yang et al. (1997) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: