Heparinase I acts on a synthetic heparin pentasaccharide corresponding to the antithrombin III binding site.
نویسندگان
چکیده
A synthetic pentasaccharide, containing an intact antithrombin III (ATIII) binding site that is in clinical studies a specific antifactor Xa agent, serves as a substrate for a heparin lyase (heparinase I, EC 4.2.2.7) from Flavobacterium heparinum. Heparinase I, currently being assessed as a heparin reversal agent, also reverses the antifactor Xa activity of this synthetic pentasaccharide by breaking it down to inactive disaccharide and trisaccharide products.
منابع مشابه
Cleavage of the antithrombin III binding site in heparin by heparinases and its implication in the generation of low molecular weight heparin.
Heparin has been used as a clinical anticoagulant for more than 50 years, making it one of the most effective pharmacological agents known. Much of heparin's activity can be traced to its ability to bind antithrombin III (AT-III). Low molecular weight heparin (LMWH), derived from heparin by its controlled breakdown, maintains much of the antithrombotic activity of heparin without many of the se...
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ورودعنوان ژورنال:
- Thrombosis research
دوره 100 6 شماره
صفحات -
تاریخ انتشار 2000