Enzymatic generation of highly anticoagulant bovine intestinal heparin

Fu, Li
Li, Kevin
Mori, Daisuke
Hirakane, Makoto
Lin, Lei
Grover, Navdeep
Datta, Payel
Yu, Yanlei
Zhao, Jing
Zhang, Fuming
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Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
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Full Citation
Enzymatic generation of highly anticoagulant bovine intestinal heparin, L. Fu, K. Li, D. Mori, M. Hirakane, L. Lin, N. Grover, P. Datta, Y. Yu, J. Zhao, F. Zhang, M. Yalcin, S. Mousa, J.S. Dordick, R.J. Linhardt, Journal of Medicinal Chemistry, 60, 8673–8679 2017.
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.
Journal of Medicinal Chemistry, 60, 8673–8679
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The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
Journal of Medicinal Chemistry