Heparinase I

Catalyzed Reaction: Heparinase I cleaves selectively, via an elimination mechanism, highly sulfated polysaccharide chains containing 1-4 linkages between hexosamines and O-sulfated iduronic acid residues. The reaction yields oligosaccharide products (mainly disaccharides) containing unsaturated uronic acids which can be detected by UV spectroscopy at 232 nm. The enzyme also cleaves the antithrombin III binding pentasaccharide domain in the heparin molecule.
Substrate Specificity: Heparin; heparan sulfate (a specific activity with heparin is approx. 3 times higher than with heparan sulfate).
Properties

Molecular weight: 42.8 kDa |
Isoelectric point: 9.3 - 9.5
pH optimum for activity: 7.4
pH range for activity: 4 - 9
Optimal temperature range: 20 ℃ – 37 ℃
Purity: ≥ 98 % by reversed-phase HPLC analysis
Protein impurities: < 0.1%
Specific Activity: > 400 IU/mg (max. 417 IU/mg)
Concentration: 10 IU/mL
Standard: 0.1 IU, 1.0 IU, or customized standard
Unit Definition: One international unit (IU) of heparinase I am defined as the amount of enzyme that will liberate 1.0 μmole unsaturated oligosaccharides from porcine mucosal heparin per minute at 35 ℃ and pH 7.0.
Stability: Expiration of heparinase I am 12 months from the manufacturing date, frozen at -20 ℃ in PBS.

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