Comparative studies of the cross-linked regions of elastin from bovine ligamentum nuchae and bovine, porcine and human aorta.
1. The preparative Edman degradation of desmosine-containing peptides permitted the isolation of peptides C-terminal to the desmosine cross-links in bovine, porcine and human aortic elastin as well as bovine ligamentum nuchae elastin. This identifies the lysines in the tropoelastin which give rise to the desmosine cross-links. 2. The sequences from bovine aortic elastin were identical with those obtained from bovine ligamentum nuchae elastin but differed from those obtained from the other species. The most striking difference involves the occurrence of phenylalanine in bovine elastin and tyrosine in porcine and human elastin C-terminal to the desmosine cross-links. 3. The sequences of the C-terminal peptides were found to fall into two distinct classes, one starting with hydrophobic residues, the other starting with alanine. It is proposed that thehydrophobic residue prevents the enzymic oxidative deamination of the adjacent lysine e-amino group and this then contributes the nitrogen to the pyridinium ring of the cross-links.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001011:Aorta / Q000032:analysis*; D002417:Cattle; D002854:Chromatography, Paper; D003895:Desmosine / Q000032:analysis; D004549:Elastin / Q000032:analysis*; D006801:Humans; D008022:Ligaments / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation; D013552:Swine
D000596:Amino Acids; D010446:Peptide Fragments; D003895:Desmosine; D004549:Elastin