The application of collagenase, purified by affintiy chromatography, to the isolation of insoluble elastin from bovine aorta.
Clostridium histolyticum collagenase (clostridiopeptidase A, EC 3.4.4.16), purified by affinity chromatography, was applied to the isolation of insoluble elastin from bovine aorta. The extremely low level of N-terminal residues (1.6 mol per 10(6) g of protein) present in this preparation indicated the almost complete lack of hydrolytic damage caused by the isolation procedure. The amino acid profile of the aortic elastin was found to be almost identical to that of insoluble elastin prepared from bovine ligamentum nuchae by the same method.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001011:Aorta / Q000032:analysis*; D001665:Binding Sites; D002417:Cattle; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D004549:Elastin / Q000302:isolation & purification; D006146:Guanidines; D006595:Hexosamines / Q000032:analysis; D003012:Microbial Collagenase / Q000302:isolation & purification; D011485:Protein Binding
D000596:Amino Acids; D006146:Guanidines; D006595:Hexosamines; D004549:Elastin; D003012:Microbial Collagenase