The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen.

  • Bächinger H
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Abstract

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.

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  • ISSN: 00219258
  • PMID: 3316229
  • PUI: 18673798
  • ISBN: 0021-9258
  • SGR: 0023657312
  • SCOPUS: 2-s2.0-0023657312

Authors

  • H. P. Bächinger

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