The chemistry of the collagen cross-links. Purification and characterization of cross-linked polymeric peptide material from mature collagen containing unknown amino acids.
A polymeric form of the alpha 1-chain C-terminal peptide alpha 1 CB6 (poly-alpha 1 CB6) was purified from CNBr digests of insoluble bovine tendon type-I-collagen by gel filtration and ion-exchage chromatography. The purified material had a molecular weight of 1.5 x 10(6)-5 x 10(6) on gel filtration and an amino acid content virtually identical with that of monomeric peptide alpha 1 CB6. The material could be adsorbed on affinity gels containing immobilized anti-(alpha 1 CB6-peptide non-helical region) antibodies and was an inhibitor of haemagglutination by the same antibodies of alpha 1 CB6-peptide-coated sheep erythrocytes. Periodate treatment of the material had no effect. Alkali hydrolysates were shown to contain two unknown amino acids, which were purified by gel filtration and ion-exchange chromatography in volatile buffers and are believed to be components of the mature cross-link of collagen.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001704:Biopolymers; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003094:Collagen; D003488:Cyanogen Bromide; D006386:Hemagglutination Tests; D010434:Pepsin A; D010446:Peptide Fragments / Q000302:isolation & purification*; D010504:Periodic Acid
D000596:Amino Acids; D001704:Biopolymers; D010446:Peptide Fragments; D010504:Periodic Acid; D003094:Collagen; D010434:Pepsin A; D003488:Cyanogen Bromide