Proteins of the periodontium

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Abstract
Summary Cyanogen bromide (CNBr) peptides were prepared of the insoluble collagen of bovine dental cementum. Following chromatographic separation, the peptides were identified by their amino-acid composition. Type I collagen ([α1(I)]2α2) accounted for more than 90% of the organic matrix, while Type III collagen ([α1(III)]3) was present at a level of approximately 5%. Amino-acid analyses revealed that the CNBr peptides from α1(I) and α2 chains of cementum closely resembled the corresponding peptides from calf skin. The only systematic difference was a higher level of hydroxylation of prolyl and lysyl residues of the cementum peptides.