Matrix proteins bound to associatively prepared proteoglycans from bovine cartilage.
Proteoglycans were extracted from bovine tracheal cartilage by high-speed homogenization, the use of dissociative solvents being avoided. The homogenate was fractionated by gel chromatography, sucrose-density-gradient centrifugation and ion-exchange chromatography. A previously unrecognized protein, cartilage matrix protein, was identified by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. It cofractionated with the proteoglycans in all systems, indicating an interaction. The cartilage matrix protein-proteoglycan complex was dissociated by treatment with 4M-guanidinium chloride. The complex again formed when the guanidine was removed. The cartilage matrix protein has a mol.wt. of more than 200000. On reduction it yields subunits with a mol.wt. of approx. 60000.
D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification*; D002356:Cartilage / Q000032:analysis*; D002417:Cattle; D002499:Centrifugation, Density Gradient; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D005260:Female; D046911:Macromolecular Substances; D008722:Methods; D008970:Molecular Weight; D011509:Proteoglycans / Q000302:isolation & purification*
D002352:Carrier Proteins; D046911:Macromolecular Substances; D011509:Proteoglycans