Collagen cross-links: location of pyridinoline in type I collagen.
Collagen from bone, dentine and tendon (type I), all of which contain the pyridinoline cross-link at varying levels, were each digested with CNBr. The resulting peptide mixtures were resolved by gel filtration on A1.5m agarose and assayed for pyridinoline. The polymeric cross-linked peptide complex, poly alpha 1CB6 [(1980) Biochem. J. 189, 111] isolated from each of these tissues did not contain pyridinoline. Only one peptide fraction contained the pyridinoline cross-link; that identified as alpha 2CB3,5. However, this peptide showed only a small increase in Mr in its cross-linked form (approx. 2000-5000) demonstrating that pyridinoline is not involved in the formation of polymeric structures like poly alpha 1CB6. These data, considered in the light of the recent finding that pyridinoline is present in type I collagens from different sources in widely varying amounts, cast doubt on its role in collagen maturation.
D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D001842:Bone and Bones / Q000032:analysis*; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D003094:Collagen / Q000032:analysis*; D003488:Cyanogen Bromide; D003804:Dentin / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D013050:Spectrometry, Fluorescence; D013710:Tendons / Q000032:analysis*
D000596:Amino Acids; D010446:Peptide Fragments; C015484:pyridinoline; D003094:Collagen; D003488:Cyanogen Bromide