Recombinant B. thetaiotaomicron Heparinase I Protein, CF

Heparin and heparan sulfate are sulfated glycosaminoglycans that share basic carbohydrate backbone structure with alternating uronic acid and N-acetylglucosamine residues (1, 2). Heparin is found in mast cells and has strong anticoagulation properties. Heparan sulfate is found on cell membrane and extracellular matrix and is involved in various biological events from cell growth, adhesion and migration to lipid metabolism. Heparin has a much higher degree of sulfation than heparan sulfate, which can be considered as a polysaccharide with regions similar to heparin interspaced with much less sulfated regions. Both heparin and heparan sulfate can be digested by heparinases, a group of bacterial lyases that are widely used as tools for processing and analyze these polysaccharides. Heparinase I from Bacteroides thetaiotaomicron (3) is a newly discovered heparinase with no activity against chondroitin sulfate and keratan sulfate (4). The enzyme readily releases tri‑sulfated and di-sulfated disaccharides from heparin and heparan sulfate.