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.
Research Article|December 01 1979
Matrix proteins bound to associatively prepared proteoglycans from bovine cartilage
Biochem J (1979) 183 (3): 539-545.
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M Paulsson, D Heinegård; Matrix proteins bound to associatively prepared proteoglycans from bovine cartilage. Biochem J 1 December 1979; 183 (3): 539–545. doi: https://doi.org/10.1042/bj1830539
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