Abstract
A large proportion of chicken bone collagen can be solubilized by denaturation at neutral pH in the solvents 5 M KCNS, 4 M CaCl 2 or 5 M LiCl. Aldimine crosslinks are absent from the solubilized collagen, and aldehyde residues, presumably released by rupture of the aldimine bonds, are now detected in the gelatin. Component α1 and α2 chains were isolated from [ 3H] borohydride-treated gelatin and digested with CNBr. The CNBr-peptides were fractionated, then analyzed for radioactivity to assess the distribution of aldehydes along each chain. A large proportion of the radioactivity eluted with the CNBr-peptides derived from the amino termini of the chains. Both hydroxynorleucine and dihydroxynorleucine were detected on analysis of the reduced peptides α1-CB1 akl and α2-CB1 akl. It is concluded that, similar to the finding for soft tissue collagens, the amino termini of α1 and α2 chains are important sites of crosslinking in bone collagen.
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