• Login
    View Item 
    •   DSpace@RPI Home
    • The Linhardt Research Labs
    • Linhardt Research Labs Papers
    • View Item
    •   DSpace@RPI Home
    • The Linhardt Research Labs
    • Linhardt Research Labs Papers
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Preparation of low molecular weight heparin from a remodeled bovine intestinal heparin

    Author
    Baytas, Sultan N.; Varghese, Sony S.; Jin, Weihua; Yu, Yanlei; He, Peng; Douaisi, Marc; Zhang, Fuming; Brodfuehrer, Paul; Xia, Ke; Dordick, Jonathan S.; Linhardt, Robert J.
    ORCID
    https://orcid.org/0000-0003-2219-5833
    Thumbnail
    Other Contributors
    Date Issued
    2021-02-25
    Subject
    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
    Preparation of low molecular weight heparin from a remodeled bovine intestinal heparin, S. N. Baytas, S. S. Varghese, W. Jin, Y. Yu, P. He, M. Douaisi, F. Zhang, P. Brodfreur, K. Xia, J. S. Dordick, R. J. Linhardt, Journal of Medicinal Chemistry, 64, 2242-2253, 2021.
    Metadata
    Show full item record
    URI
    https://doi.org/10.1021/acs.jmedchem.0c02019; https://hdl.handle.net/20.500.13015/5457
    Abstract
    Bovine intestinal heparins are structurally distinct from porcine intestinal heparins and exhibit lower specific anticoagulant activity (units/mg). The reduced content of N-sulfo, 3-O-sulfo glucosamine, the central and critical residue in heparin’s antithrombin III binding site, is responsible for bovine intestinal heparin’s reduced activity. Previous studies demonstrate that treatment of bovine intestinal heparin with 3-O-sulfotransferase in the presence of 3′-phosphoadenosine-5′-phosphosulfate afforded remodeled bovine heparin with an enhanced activity reaching the United States Pharmacopeia’s requirements. Starting from this remodeled bovine intestinal heparin, we report the preparation of a bovine intestinal low molecular weight heparin having the same structural properties and anti-factor IIa and anti-factor Xa activities of Enoxaparin. Moreover, this bovine intestinal heparin-derived “Enoxaparin” showed comparable platelet factor-4 binding affinity, suggesting that it should exhibit similarly low levels of heparin induced thrombocytopeneia, HIT.;
    Description
    Journal of Medicinal Chemistry, 64, 2242-2253; 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);
    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.0c02019;
    Collections
    • Linhardt Research Labs Papers

    Browse

    All of DSpace@RPICommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

    My Account

    Login

    DSpace software copyright © 2002-2022  DuraSpace
    Contact Us | Send Feedback
    DSpace Express is a service operated by 
    Atmire NV