Bovine type I collagen: A study of cross-linking in various mature tissues.
The cyanogen bromide peptides from insoluble and pepsin solubilised type I collagen of bovine bone, dentine, meniscus, tendon, skin and cornea were compared by SDS-polyacrylamide gel electrophoresis. In each case alpha 1CB6 was shown to be the only peptide of molecular weight greater than 10 000 involved in cross-linking. The major helical peptides alpha 1CB3, alpha 1CB8, alpha 1CB7 and alpha 2CB4 were not implicated in cross-linking in any tissue either by end overlap or helix-helix interaction. The C-terminal alpha 2 chain peptide alpha 2CB3,5, 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.
D000818:Animals; D001842:Bone and Bones / Q000032:analysis; D002417:Cattle; D003094:Collagen / Q000302:isolation & purification; D003315:Cornea / Q000032:analysis; D003804:Dentin / Q000032:analysis; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000032:analysis; D012867:Skin / Q000032:analysis; D013710:Tendons / Q000032:analysis; D014018:Tissue Distribution
D046911:Macromolecular Substances; D010446:Peptide Fragments; D003094:Collagen