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Interaction of Fibronectin and Its Proteolytic Fragments with Hyaluronic Acid1
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1982
Year
Tissue EngineeringEngineeringCell AdhesionGlycobiologyBiomedical EngineeringAffinity ChromatographyHyaluronic Acid1Protein FoldingBioanalysisClinical ChemistryMatrix BiologyConnective Tissue DiseaseFibrosisBiochemistryCell BiologyHyaluronic AcidPorcine Plasma FibronectinCell-matrix InteractionWound HealingMedicineExtracellular Matrix
The interaction of porcine plasma fibronectin and its proteolytic fragments with hyaluronic acid was investigated by affinity chromatography using hyaluronic acid-linked Sepharose 4B. Hyaluronic acid was found to interact with all major fragments including the gelatin-binding polypeptide which has no affinity for heparin. A difference between hyaluronic acid and heparin was also noted in the relative interaction with two larger fragments. This type of multiple interaction may account for the affinity for hyaluronic acid strong enough to prevent the elution of fibronectin from the hyaluronate-column with a buffer containing 2 M NaCl.