Chains of matrix-derived type X collagen: size and aggregation properties.
Type X collagen was isolated from extracts of embryonic chick cartilages by immunoprecipitation and subsequently analyzed by SDS-PAGE. Most of the chains migrated with a molecular weight of 59 kDa, suggesting that the matrix form of type X collagen has not undergone post-secretory proteolytic processing. Minor amounts of material were also observed at 120 kDa, 70 kDa and 50 kDa. These were dimers or limited proteolytic products of type X chains.
Schmid
T M
TM
Department of Biochemistry, Rush Presbyterian-St. Luke's Med. Ctr., Chicago, IL.
Linsenmayer
T F
TF
D000818:Animals; D000911:Antibodies, Monoclonal; D001857:Bone Matrix / Q000032:analysis*; D002356:Cartilage / Q000032:analysis; D002642:Chick Embryo; D003094:Collagen / Q000032:analysis* / Q000276:immunology; D004591:Electrophoresis, Polyacrylamide Gel; D011233:Precipitin Tests
D000911:Antibodies, Monoclonal; D003094:Collagen