Purification of a mucopolysacharidase from Bacteroides distasonis.
A mucopolysaccharidase derived from a pathogenic strain of Bacteroides distasonis was isolated and purified by fractionation with cold acetone and ion-exchange chromatography on DEAE-cellulose, pH 8.0. Three detectable enzyme activities from concentrated supernatant filtrates were obtained in a fraction precipitated by three volumes of cold acetone; these were DNAase, hyaluronidase and chondroitinase-like activity. Separation of the DNAase was achieved by ion-exchange chromatography. Fractions designated as purified mucopolysaccharidase contained both hyaluronidase and chondroitinase-like activity.
D001439:Bacteroides / Q000201:enzymology* / Q000472:pathogenicity; D002810:Chondroitinases and Chondroitin Lyases / Q000302:isolation & purification; D002852:Chromatography, Ion Exchange; D003851:Deoxyribonucleases / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D005966:Glucuronidase / Q000302:isolation & purification*; D006821:Hyaluronoglucosaminidase / Q000302:isolation & purification; D008190:Lyases / Q000302:isolation & purification*
C021812:mucopolysaccharidase; D003851:Deoxyribonucleases; D005966:Glucuronidase; D006821:Hyaluronoglucosaminidase; D008190:Lyases; D002810:Chondroitinases and Chondroitin Lyases