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.
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© 1977 Plenum Press, New York
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Lamy, F., Gibson, D., Ledoux, M., Moreux, J.C. (1977). Chymotrypsinogen D, A New Zymogen from Porcine Pancreas with Proelastolytic Activity. In: Sandberg, L.B., Gray, W.R., Franzblau, C. (eds) Elastin and Elastic Tissue. Advances in Experimental Medicine and Biology, vol 79. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-9093-0_15
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DOI: https://doi.org/10.1007/978-1-4684-9093-0_15
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