Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:Chymotrypsinogen D, a new zymogen from porcine pancreas with proelastolytic activity. 86 35

Two porcine pancreatic zymogens can be separated by free electrophoresis on a sucrose gradient. After activation by trypsin, both enzymes can hydrolyze completely the fibrous protein elastin. One of the two proteins, proelastase B, has, in addition, an esterolytic activity towards N-acetyl-L-tyrosine ethyl ester. The other, proelastase A, does not possess it. The activation products of the zymogens have been tagged with radioactive diisopropylfluro-phosphonate and separated by polacrylamide-gel electrophoresis. Proelastase A gives only one active species, pancreatopeptidase E, but three distinct proteins can be obtained from proelastase B. Elastases A and B exhibit an important synergism when acting together upon a purified elastin lacking microfibrils. Trypsin has considerably less synergistic activity, and chymotrypsin has practically none.
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PMID:Electrophoretic characterization of porcine pancreatic (pro)elastases A and B. 112 26