Purification and characterization of the low-molecular-mass (type X) collagen from chick-embryo tibial cartilage.
Type X collagen, synthesized in large amount by cultured tibial chondrocytes, is deposited in vivo in the epiphyseal cartilages of 17-day-old chick embryo tibiae. Here we report the extraction of this collagen from these cartilages by limited pepsin digestion and its purification to electrophoretic homogeneity by salt precipitation followed by agarose gel filtration. Identity of the collagen purified from cartilage with the type X collagen synthesized by cultured chondrocytes is confirmed by comparison of the amino acid compositions. The high glycosylation extent of type X collagen is reminiscent of the glycosylation extent of pericellular collagens. The possible role of type X collagen is discussed.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D002356:Cartilage / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D002642:Chick Embryo; D002850:Chromatography, Gel; D003094:Collagen / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D013977:Tibia / Q000032:analysis
D000596:Amino Acids; D002241:Carbohydrates; D003094:Collagen