Enzymatic Generation of Highly Anticoagulant Bovine Intestinal Heparin
JOURNAL OF MEDICINAL CHEMISTRY, vol.60, no.20, pp.8673-8679, 2017 (SCI-Expanded, Scopus)
- Publication Type: Article / Article
- Volume: 60 Issue: 20
- Publication Date: 2017
- Doi Number: 10.1021/acs.jmedchem.7b01269
- Journal Name: JOURNAL OF MEDICINAL CHEMISTRY
- Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Page Numbers: pp.8673-8679
- Bursa Uludag University Affiliated: Yes
Abstract
Unlike USP porcine heparin, bovine intestinal heparin (BIH) has a low anticoagulant activity. Treatment with 6-OST-1,-3, and/or 3-OST-1 afforded two remodeled heparins that met USP heparin activity and Mw specifications. We explored the pharmacodynamics and pharmacokinetics in a rabbit model. We conclude that a modest increase in the content of 3-O-sulfo groups in BIH increases the number of antithrombin III binding sites, making remodeled BIH behave similarly to pharmaceutical heparin.