title: Chymotrypsinogen D, a new zymogen from porcine pancreas with proelastolytic activity.
abstract: During the purification of propancreatopeptidase E, a proATEEase activity is always copurified. The proelastolytic 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.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002919:Chymotrypsinogen / Q000302:isolation & purification / Q000378:metabolism; D004549:Elastin / Q000378:metabolism*; D004792:Enzyme Precursors / Q000302:isolation & purification / Q000378:metabolism; D007328:Insulin / Q000378:metabolism; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000302:isolation & purification / Q000378:metabolism; D013552:Swine
chemical_list: D004792:Enzyme Precursors; D007328:Insulin; D004549:Elastin; D002919:Chymotrypsinogen; D010196:Pancreatic Elastase