title: Embryonic chick cartilage collagens. Differences in the low-Mr species present in sternal cartilage and tibiotarsal articular cartilage.
abstract: The collagenous polypeptides present in embryonic chick sternal and tibiotarsal cartilages have been solubilised by digestion with pepsin and separated by salt fractionation. Type II collagen, 1 alpha 2 alpha 3 alpha collagen, and two polypeptides (apparent molecular mass 150 and 42 kDa), which were reducible to a number of smaller peptides, were extracted from both tissues. However, also present in the peptic digests of tibiotarsal cartilages was a major non-reducible highly-soluble polypeptide of 45 kDa. This short-chain collagen is apparently identical to the pepsinized product of G collagen (Mr 59 000), a major low-Mr procollagen-like species previously detected in chick chondrocyte cultures.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002356:Cartilage / Q000032:analysis*; D002358:Cartilage, Articular / Q000032:analysis; D002642:Chick Embryo; D003094:Collagen / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D008854:Microscopy, Electron; D008970:Molecular Weight; D010434:Pepsin A / Q000378:metabolism
chemical_list: D000596:Amino Acids; D003094:Collagen; D010434:Pepsin A