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Affinity binding of the cartilage proteo glycan protein keratan sulfate core to immobilized hyaluronic acid



Affinity binding of the cartilage proteo glycan protein keratan sulfate core to immobilized hyaluronic acid



Analytical Biochemistry 90(1): 22-32



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.degree. C. After the digested chondroitin sulfate chains were washed from the column, the bound protein-keratan sulfate core was eluted with 4 M 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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Accession: 004685176

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PMID: 153111


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