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  • Title: Bovine periodontal ligament. An invesitation of the collagen, glycosaminoglycan and insoluble glycoprotein components at different stages of tissue development.
    Author: Pearson CH, Wohllebe M, Carmichael DJ, Chovelon A.
    Journal: Connect Tissue Res; 1975; 3(4):195-206. PubMed ID: 126133.
    Abstract:
    Periodontal ligaments from unerupted, partially erupted and mature teeth were extracted with 0.15 M NaCl. The major reducible collagen cross-link in each insoluble fraction was dehydrodihydroxylysinonorleucine; the dehydroydroxylysinonorleucine contents were smaller. There was no significant difference in the quantities of these cross-links relative to collagen contents in the three speciments, but one of the precursors, hydroxyallysine, markedly decreased in the older tissue. The amino acid compositions of the trypsin-resistant insoluble fractions were generally characteristic of collagen. Analyses of separated glycopeptides revealed the presence of insoluble non-collagenous glycoproteins and collagen hexoses. The latter were lower in the mature ligament. Hyaluronic acid progressively decreased relative to chondroitin sulphate on eruption and maturation. A hyaluronidase-resistant glycosaminoglycan, probably dermatan sulphate, occurred in the NaCl-insoluble fraction of the mature ligament and in appreciable amounts in all NaCl extracts.
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