Enzymatic generation of highly anticoagulant bovine intestinal heparin

Authors
Fu, Li
Li, Kevin
Mori, Daisuke
Hirakane, Makoto
Lin, Lei
Grover, Navdeep
Datta, Payel
Yu, Yanlei
Zhao, Jing
Zhang, Fuming
ORCID
https://orcid.org/0000-0003-2219-5833
No Thumbnail Available
Other Contributors
Issue Date
2017-10-26
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
Terms of Use
In Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
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.
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.
Description
Journal of Medicinal Chemistry, 60, 8673–8679
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
Journal of Medicinal Chemistry
https://harc.rpi.edu/
Access
https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1021/acs.jmedchem.7b01269