Bacteroides Heparinase I
Supplier: W.u.G. Dickgießer GmbHTotal Ratings: 0
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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. Bacteroides Heparinase I cleaves the glycosidic bond between N-sulfated hexosamines and 2-O-sulfated iduronic acid 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. Bacteroides Heparinase I cleaves 2-O sulfated iduronic acid and 2-O sulfated glucuronic acid residues at similar rates. Limited digest of porcine mucosal heparin with the Bacteroides Heparinase I results in heparin oligosaccharides with a lower extent of sulfation as reported.
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