Birkedal-Hansen H, Butler W T, Taylor R E
Calcif Tissue Res. 1977 May 31;23(1):39-44. doi: 10.1007/BF02012764.
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 ([alpha1(I)]2alpha2) accounted for more than 90% of the organic matrix, while Type III collagen ([alpha1(III)]3) was present at a level of approximately 5%. Amino-acid analyses revealed that the CNBr peptides from alpha1(I) and alpha2 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.
