Bacteroides Heparinase I
Bacteroides Heparinase I cloned from Bacteroides eggerthii, also called Heparin Lyase I, is active on heparin and the highly sulfated domains of heparan sulfate. The reaction yields oligosaccharide products containing unsaturated uronic acids which can be detected by UV spectroscopy at 232 nm.
In contrast to the Flavobacterium heparinum Heparinase I which cleaves the glycosidic bond between N-sulfated hexosamines and 2-O-sulfated iduronic acid residues, the Bacteroides Heparinase I cleaves between these same residues as well as the 2-O-sulfated glucuronic acid residues. The 2-O-sulfated uronic acid residue is essential for the activity of Bacteroides Heparinase I and 6-O-sulfation of GlcNS does not hinder enzyme activity. While Bacteroides Heparinase I cleaves 2-O sulfated iduronic acid and 2-O sulfated glucuronic acid residues at similar rates, the Flavobacterium heparinum Heparinase I has a much higher rate of cleavage for 2-O sulfated iduronic acid residues (1). Limited digest of porcine mucosal heparin with Flavobacterium heparinum Heparinase I results in sulfated heparin oligosaccharides structures previously reported (2). Limited digest of porcine mucosal heparin with the Bacteroides Heparinase I results in heparin oligosaccharides with a lower extent of sulfation as reported (3).
Product SourceCloned from Bacteroides Eggerthii and expressed in E. coli.
The following reagents are supplied with this product:
Store at (°C) Concentration Bacteroides Heparinase Reaction Buffer (10X) -20 10 X
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