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pubmed:abstractText |
A mucopolysaccharidase in the cell extract of an oral strain of Bacteroides sp. was purified to homogeneity by ammonium sulfate precipitation, DEAE-cellulose column chromatography, gel filtration on Sephadex G-200, and isoelectric focusing. Specific activity increased 110-fold and recovery was 2%. The molecular weight was determined to be 89,000 by gel filtration, and the isoelectric point was 7.0. The optimum pH for the activity was 6.5. The enzyme was inactivated by heating at 60 degrees C for 5 min. The purified mucopolysaccharidase degraded hyaluronic acid more rapidly than chondroitin and chondroitin sulfate A and C. However, it had no activity against chondroitin sulfate B, heparin, and heparan sulfate. Since unsaturated disaccharides were derived from the enzyme substrate, this enzyme was considered to be a mucopolysaccharide lyase.
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