The covalent structure of the first 111 residues from the N -terminus of peptide α1(II)-CB10 from bovine nasal-cartilage collagen is presented. This region comprises residues 552–661 of the α1(II) chain. The sequence was determined by automated Edman degradation of peptide α1(II)-CB10 and of peptides produced by cleavage with trypsin and hydroxylamine. Comparison of this region of the α1(II) chain with the homologous segment of the α1(I) chain indicated a homology level of 85%, slightly higher than that of 81% reported for the N -terminal region of the α1(II) chain (Butler, Miller & Finch (1976) Biochemistry 15 , 3000–3006). The occurrence of two residues of glycosylated hydroxylysine was established at positions 564 and 603, the first present exclusively as galactosylhydroxylysine and the latter as a mixture of galactosylhydroxylysine and glucosylgalactosylhydroxylysine. Also, two residues at positions 648 and 657 were tentatively identified as glycosylated hydroxylysines. The amino acid sequences adjacent to the hydroxylysine residues so far identified in the α1(II) chain were compared with the homologous regions of the α1(I) and α2 chains, but no obvious prerequisite for hydroxylation could be seen. From comparison with the homologous sequence of the α1(I) chain, it appears that the α1(II)-chain sequence presented here contains three more amino acids than that reported for the α1(I) chain. This triplet would be interposed between residues 63 and 64 of the reported sequence of peptide α1(I)-CB7 from calf skin collagen. Data on the purification of the subpeptides and their amino acid compositions have been deposited as Supplementary Publication SUP 50087 (7 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169 , 5.
1. Elastins purified by various methods from the ligamentum nuchae and the lungs of cattle of various ages were analysed for amino acid compositions and lysine-derived cross-links. 2. In fully mature elastins from adults the main cross-links were desmosine, isodesmosine and lysinonorleucine and the so-called aldol-condensation product. Trace amounts of merodesmosine were also found. 3. During the normal maturation of elastins the amounts of desmosine, isodesmosine and lysinonorleucine increased, whereas the aldol-condensation product and intact lysine residues decreased and merodesmosine remained the same. 4. Elastins from young animals contained significant amounts of dehydromerodesmosine whereas elastins from adults contained virtually nil. Evidence is presented which suggests that the biosynthetic pathway of desmosine and isodesmosine proceeds via the aldol-condensation product and dehydromerodesmosine.