Interaction of mucopolysaccharides with glycosaminoglycans on glycosaminoglycan-bound AH-Sepharose 4B.
Chondroitinase C, chondroitinase AC, heparinase, and heparitinase separated from an extract of Flavobacterium heparinum were subjected to affinity chromatography with glycosaminoglycan-bound AH-Sepharose 4B, previously coated non-covalently with glycosaminoglycan, as the matrix. The results suggested the importance of coating the matrix with glycosaminoglycan in the binding of the enzyme protein to the matrix.
D002810:Chondroitinases and Chondroitin Lyases / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000378:metabolism*; D005417:Flavobacterium / Q000201:enzymology*; D006025:Glycosaminoglycans; D006493:Heparin; D006497:Heparan Sulfate; D011133:Polysaccharide-Lyases / Q000378:metabolism*; D012685:Sepharose
D002810:Chondroitinases and Chondroitin Lyases; D004800:Enzymes, Immobilized; D006025:Glycosaminoglycans; D006493:Heparin; D006497:Heparan Sulfate; D011133:Polysaccharide-Lyases; D012685:Sepharose