Identification of disulphide-bonded type X procollagen polypeptides in embryonic chick chondrocyte cultures.
A high-Mr (Mr 120,000), disulphide-bonded collagenous polypeptide was observed to co-purify with the prox1(X) chain during isolation of cartilage collagens from culture medium of embryonic chick tibiotarsal chondrocytes. This high Mr polypeptide was subsequently shown by two-dimensions l SDS-PAGE and peptide mapping to represent a dimer of the prox1(X) chain of type X collagen linked by disulphide bonding in the non-collagenous domains.
D000818:Animals; D002356:Cartilage / Q000032:analysis* / Q000166:cytology; D002478:Cells, Cultured; D055598:Chemical Phenomena; D002621:Chemistry; D002642:Chick Embryo; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis; D011347:Procollagen / Q000032:analysis*
D010455:Peptides; D011347:Procollagen