Proteolysis of tropoelastin.
The presence of an enzyme associated with tropoelastin is described. The enzyme has a pH optimum between 7 and 9 and trypsin-like specificity. Upon incubation, tropoelastin (72,000 molecular weight) is cleaved into relatively high molecular weight fragments. In addition to the parent molecule, five discrete polypeptide bands are usually observed on SDS gels with molecular weights of approximately 57,000, 45,000, 36,000, 25,000 and 13-14,000.
D000629:Aminopropionitrile; D000818:Animals; D002614:Chelating Agents / Q000494:pharmacology; D002645:Chickens; D004549:Elastin / Q000031:analogs & derivatives*; D010450:Endopeptidases / Q000378:metabolism*; D008970:Molecular Weight; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D011480:Protease Inhibitors; D011485:Protein Binding; D013439:Sulfhydryl Reagents / Q000494:pharmacology; D014106:Tosylarginine Methyl Ester / Q000378:metabolism; D014107:Tosyllysine Chloromethyl Ketone / Q000494:pharmacology; D014108:Tosylphenylalanyl Chloromethyl Ketone / Q000494:pharmacology; D014333:Tropoelastin / Q000378:metabolism*
D002614:Chelating Agents; D011480:Protease Inhibitors; D013439:Sulfhydryl Reagents; D014333:Tropoelastin; D000629:Aminopropionitrile; D014107:Tosyllysine Chloromethyl Ketone; D014108:Tosylphenylalanyl Chloromethyl Ketone; D004549:Elastin; D014106:Tosylarginine Methyl Ester; D010450:Endopeptidases; D010196:Pancreatic Elastase