Chymotrypsinogen D, A New Zymogen from Porcine Pancreas with Proelastolytic Activity
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.
KeywordsPorcine Pancreas Performic Acid Partial Specific Volume Elastolytic Activity Esterolytic Activity
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