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Chymotrypsinogen D, A New Zymogen from Porcine Pancreas with Proelastolytic Activity

  • F. Lamy
  • D. Gibson
  • M. Ledoux
  • J. C. Moreux
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 79)

Abstract

During the purification of propancreatopeptidase E, a proATEEase activity is always copurified. The pro-elastolytlc and proesterolytic activities can be separated on a hydroxylapatite column. The zymogen with potential ATEEase activity has a basic isoelectric point, can be activated by trypsin, and can hydrolyse elastin and ATEE but not ATAME. Its molecular weight is about 26,500 and the NH2-terminal sequence indicates clearly that it belongs to the chymotrypsinogen family, but that it is not chymotrypsinogen A, B, or C. We call it chymotrypsinogen D. Although both pancreatopeptidase E and chymotrypsin D can hydrolyse elastin, the synthetic substrate ATAME is attacked only by pancreatopeptidase E. Therefore, the peptide bonds in elastin cleaved by these two enzymes should be different.

Keywords

Porcine Pancreas Performic Acid Partial Specific Volume Elastolytic Activity Esterolytic Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • F. Lamy
    • 1
  • D. Gibson
    • 1
  • M. Ledoux
    • 1
  • J. C. Moreux
    • 1
  1. 1.Departement de Biochimie, Faculte de MedecineUniversite de SherbrookeSherbrookeCanada

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