Peptidyl-prolyl cis-trans isomerase was extracted from pig kidney cortex and partially purified. Enzyme activity was monitored against the cis-trans isomerization of succinyl-Ala-Ala-Pro-Phe-methylcoumaryl amide by means of a two-step process using chymotrypsin as the trans cleaving activity. The in vitro refolding of denatured type III collagen, which is rate-limited by the cis-trans isomerization of peptide bonds, was studied in the presence of peptidyl-prolyl cis-trans isomerase by optical rotatory dispersion and by resistance to tryptic digestion. A 3-fold increase in the initial rate of folding was observed compared to the uncatalyzed refolding. This rate increase is comparable to the rate increase found for the CT-phase in the refolding of urea-denatured ribonuclease A, but it is smaller than the increase in the rate of isomerization of succinyl-Ala-Ala-Pro-Phe-methylcoumarylamide.
CITATION STYLE
Bächinger, H. P. (1987). The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen. The Journal of Biological Chemistry, 262(35), 17144–17148. https://doi.org/10.1016/s0021-9258(18)45502-0
Mendeley helps you to discover research relevant for your work.