Bovine periodontal ligament. An invesitation of the collagen, glycosaminoglycan and insoluble glycoprotein components at different stages of tissue development.

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.