BOVINE TYPE-I COLLAGEN - STUDY OF CROSS-LINKING IN VARIOUS MATURE TISSUES

The cyanogen bromide peptides from insoluble and pepsin solubilised type 1 collagen of bovine bone, dentine, meniscus, tendon, skin and cornea were compared by SDS-polyacrylamide gel electrophoresis. In each case α1CB6 was shown to be the only peptide of molecular weight greater than 10 000 involved in cross-linking. The major helical peptides α1CB3, α1CB8, α1CB7 and α2CB4 were not implicated in cross-linking in any tissue either by end overlap or helix-helix interaction. The C-terminal α2 chain peptide α2CB3,5, which contains a large helical region, was not involved in cross-linking to any large peptides, although a slight increase in molecular weight in all tissues examined did suggest a possible interaction(s) with a very small peptide of molecular weight 4-5000. © 1979.