Heparinase I cleaves heparin and heparan sulfate (relative activity about 3:1) at the linkages between hexosamines and O-sulfated iduronic acids, yiel…
Heparinase I cleaves heparin and heparan sulfate (relative activity about 3:1) at the linkages between hexosamines and O-sulfated iduronic acids, yielding mainly disaccharides. The enzyme also cleaves the antithrombin III binding pentasaccharide domain in the heparin molecule. Recombinant Heparinase I from Flavobacterium heparinum; Host Cell: E. Coli. Property l pH stability 6.5-7.5 l Optimum pH 7.0 l Thermal stability ≤35℃(pH7.0, 20min) l Optimum temperature 35℃ l Molecular weight 42,508 l Isoelectric point 9.4 Specification l Specific activity >100 IU/mg. Enzyme activity definition One Heparinase I international unit (IU) is defined as the amount of enzyme that will liberate 1.0 μmole unsaturated oligosaccharides from porcine intestinal mucosal heparin per minute at 30℃ and pH 7.0.
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