Proteins of the periodontium. Identification of collagens with the [alpha1(I)]2alpha2 and [alpha1(III)]3 structures in bovine periodontal ligament.
Insoluble collagen was prepared from bovine periodontal ligament. Isolation and characterization of CNBr peptides originating from the alpha1(I), alpha2, and alpha1(III) chains showed that the tissue contained both type I and type III collagens. Further evidence for the presence of type III collagen was obtained by the isolation of alpha1(III) chains from pepsin-treated ligament collagen, with properties similar to those of human alpha1(III) chains. Estimates based on the amounts of certain CNBr peptides indicated that about one-fifth of the collagen of periodontal ligament is type III, the remainder being type I collagen.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003094:Collagen / Q000032:analysis*; D008022:Ligaments / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D010519:Periodontium / Q000032:analysis*
D000596:Amino Acids; D010446:Peptide Fragments; D003094:Collagen