Identification of the cartilage alpha 1(XI) chain in type V collagen from bovine bone.
Type V collagen prepared from bovine bone was resolved into three distinct alpha-chains by high performance liquid chromatography and gel electrophoresis. Peptide mapping established two chains as alpha 1(V) and alpha 2(V) as expected and the third as the cartilage alpha 1(XI) chain (previously thought to be unique to cartilage). In adult bone, the type V collagen fraction was richer in alpha 1(XI) chains than in fetal bone (about 1/3 of the chains in the adult). How these polypeptides are organized into native molecules is not yet clear, though the stoichiometry suggests cross-type heterotrimers between the type V and XI chains.
Niyibizi
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Department of Orthopaedics, University of Washington, Seattle 98195.
Eyre
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D000818:Animals; D001842:Bone and Bones / Q000032:analysis*; D002356:Cartilage / Q000032:analysis*; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D003094:Collagen / Q000032:analysis* / Q000145:classification; D004591:Electrophoresis, Polyacrylamide Gel
D003094:Collagen