Abstract
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.
Highlights
Insoluble collagen was prepared from bovine periodontal ligament
The bovine dentition proved to be a source of sufficient material for detailed biochemical characterization of periodontal ligament collagen (PDL) collagen
Extraction of the freshly excised PDL with 1.0 M NaCl in 0.05 M Tris-HCl buffer removed about 10% of the dry weight but only 0.9% of the collagen
Summary
Isolation and characterization of CNBr peptides originating from the al(I), cu, and (~l(I11) chains showed that this tissue contained both type I and type III collagens. Further evidence for the presence of type III collagen was obtained by the isolation of (~l(I11) chains from pepsin-treated periodontal ligament collagen, with properties similar to those of human (ul(II1) 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. Type III collagen with the structure [al(III)], occurs in a number of tissues along with type I collagen [6,7,8]. This report describes the isolation and characterization of the CNBr peptides from the insoluble collagen of bovine PDL and the isolation of ~ul(II1) chains from pepsin-treated material. A preliminary report of this research was published [9]
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