Affinity binding of the cartilage proteoglycan protein-keratan sulfate core to immobilized hyaluronic acid. |
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Authors: | J E Christner M L Brown D D Dziewiatkowski |
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Institution: | 1. Department of Oral Biology, The University of Michigan, Ann Arbor, Michigan 48109 USA;2. Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109 USA;3. The Dental Research Institute, The University of Michigan, Ann Arbor, Michigan 48109 USA |
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Abstract: | The protein-keratan sulfate core of bovine nasal cartilage proteoglycan was purified by affinity chromatography on a column of immobilized hyaluronic acid. The hyaluronic acid was immobilized by reaction with a hydrazido-alkyl derivative of Sepharose in the presence of borohydride. Proteoglycan was digested with chondroitinase ABC and the entire mixture was passed over a column of the Sepharose-hyaluronic acid maintained at 4°C. After the digested chondroitin sulfate chains were washed from the column, the bound protein-keratan sulfate core was eluted with 4m guanidinium chloride. The protein-keratan sulfate core interacts with the affinity matrix through its hyaluronic acid binding site as shown by the inhibition of binding by free hyaluronic acid and hyaluronic acid decasaccharide. |
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