Isolation of a glycoprotein and proteodermatan sulphate from bovine achilles tendon by affinity chromatography on concanavalin A-Sepharose.
A fraction was isolated from a 3 M MgCl2 extract of bovine achilles tendon on the basis of its affinity for collagen. Affinity chromatography of this material on concanavalin A-Sepharose yielded a mixture which comprised a glycoprotein of approximate molecular weight 60 000 and two constituents containing hexuronic acid. The existence of a complex between the glycoprotein and material containing hexuronic acid was demonstrated by chromatography on Sephadex G-200 and by equilibrium sedimentation in CsCl density gradients. The complex was completely dissociated in 4 M guanidinium chloride. One of the constituents containing hexuronic acid was identified as a proteodermatan sulphate of low molecular weight and which had an abnormally high protein content (45-50%) and low buoyant density (1.46 g/ml) for a proteoglycan. The denser of the two molecules containing hexuronic acid appeared to be a normal proteoglycan, with a low protein content (11%). Analyses are given for the glycoprotein and the proteodermatan sulphate.
D000125:Achilles Tendon / Q000032:analysis*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002499:Centrifugation, Density Gradient; D002807:Chondroitin / Q000031:analogs & derivatives*; D002846:Chromatography, Affinity; D002849:Chromatography, Gas; D003208:Concanavalin A; D003871:Dermatan Sulfate; D004589:Electrophoresis, Disc; D006023:Glycoproteins / Q000302:isolation & purification*; D006601:Hexoses / Q000032:analysis; D006603:Hexuronic Acids / Q000032:analysis; D011485:Protein Binding; D012685:Sepharose
D000596:Amino Acids; D006023:Glycoproteins; D006601:Hexoses; D006603:Hexuronic Acids; D003208:Concanavalin A; D003871:Dermatan Sulfate; D002807:Chondroitin; D012685:Sepharose