title: Purification and properties of Bacteroides heparinolyticus heparinase (heparin lyase, EC 4.2.2.7).
abstract: Heparinase (heparin lyase, EC 4.2.2.7) was isolated from the cell extract of an oral bacterium, Bacteroides heparinolyticus. It was a basic protein with an isoelectric point of 9.5. Its molecular weight was 63,000. The enzyme was the most active against heparin among the tested mucopolysaccharides. Catalytic properties may be similar to those of heparinase of Flavobacterium heparinum, since the enzymatic degradation products obtained by using the two enzymes were the same on the basis of paper chromatography.
authors.affiliation: Department of Oral Microbiology, Matsumoto Dental College, Nagano-Prefecture, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Nakamura
authors.forename: Y
authors.initials: Y
authors.lastname: Shibata
authors.forename: S
authors.initials: S
authors.lastname: Fujimura
mesh_terms: D001439:Bacteroides / Q000201:enzymology*; D002854:Chromatography, Paper; D004591:Electrophoresis, Polyacrylamide Gel; D019763:Heparin Lyase; D007525:Isoelectric Focusing; D011133:Polysaccharide-Lyases / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D011133:Polysaccharide-Lyases; D019763:Heparin Lyase