Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 549-556 |
| Number of pages | 8 |
| Journal | Thrombosis Research |
| Volume | 100 |
| Issue number | 6 |
| DOIs | |
| State | Published - 15 Dec 2000 |
| Externally published | Yes |
Keywords
- Heparin lyase
- Heparinase
- Neutralization
- Pentasaccharide
- Reversal
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