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    Antithrombin III Binding Site Analysis of Low Molecular Weight Heparin Fractions

    Author
    Chen, Yin; Zhao, Jing; Yu, Yanlei; Liu, Xinyue; Lin, Lei; Zhang, Fuming; Linhardt, Robert J.
    ORCID
    https://orcid.org/0000-0003-2219-5833
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    Other Contributors
    Date Issued
    2018-05-01
    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
    Antithrombin III Binding Site Analysis of Low Molecular Weight Heparin Fractions, Y Chen, J Zhao, Y Yu, X Liu, L Lin, F Zhang, R. J. Linhardt, Journal of Pharmaceutical Sciences, 107, 1290-1295, 2018.
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    URI
    https://doi.org/10.1016/j.xphs.2018.01.008; https://hdl.handle.net/20.500.13015/5594
    Abstract
    Low-molecular-weight heparins (LMWHs) are widely used as clinical anticoagulant drugs. LMWHs are heterogeneous and highly negatively charged glycans prepared by chemical or enzymatic depolymerization of unfractionated heparin. The detailed structural analysis of a LMWH is essential for the drug quality control. In this study, an LMWH, enoxaparin sodium (a generic version of Lovenox) was separated into different molecular weight fractions by a Superdex peptide column. The disaccharide compositions, 3-O-sulfo group-containing tetrasaccharides composition, and antithrombin III-binding affinity of the fractions from this LMWH were analyzed. The results showed that all the fractions had very similar disaccharide and 3-O-sulfo group-containing tetrasaccharide compositions, but the fraction containing larger-sized chains had higher antithrombin III-binding affinity.;
    Description
    Journal of Pharmaceutical Sciences, 107, 1290-1295; 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 Pharmaceutical Sciences; https://harc.rpi.edu/;
    Access
    https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/j.xphs.2018.01.008;
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