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    Structural Analysis of Heparin-Derived 3-O-Sulfated Tetrasaccharides: Antithrombin Binding Site Variants

    Author
    Chen, Yin; Lin, Lei; Agyekum, Isaac; Zhang, Xing; St. Ange, Kalib; Yu, Yanlei; Zhang, Fuming; Liu, Jian; Amster, I. Jonathan; Linhardt, Robert J.
    ORCID
    https://orcid.org/0000-0003-2219-5833
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    STRUCTURAL ANALYSIS OF HEPARIN-DERIVED 3-O-SULFATEDSTRUCTURAL ANALYSIS OF HEPARIN-DERIVED 3-O-SULFATED.pdf (1.042Mb)
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    Date Issued
    2017-04-01
    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
    Structural Analysis of Heparin-Derived 3-O-Sulfated Tetrasaccharides: Antithrombin Binding Site Variants, Y. Chen, L. Lin, I. Agyekum, X. Zhang, K. St.Ange, Y. Yu, J. Liu, I. J. Amster, R. J. Linhardt, Journal of Pharmaceutical Sciences, 106, 973-981, 2017.
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    URI
    https://hdl.handle.net/20.500.13015/5387; https://doi.org/10.1016/j.xphs.2016.11.023
    Abstract
    Heparin is a polysaccharide that is widely used as an anticoagulant drug. The mechanism for heparin's anticoagulant activity is primarily through its interaction with a serine protease inhibitor, antithrombin III (AT), that enhances its ability to inactivate blood coagulation serine proteases, including thrombin (factor IIa) and factor Xa. The AT-binding site in the heparin is one of the most well-studied carbohydrate-protein binding sites and its structure is the basis for the synthesis of the heparin pentasaccharide drug, fondaparinux. Despite our understanding of the structural requirements for the heparin pentasaccharide AT-binding site, there is a lack of data on the natural variability of these binding sites in heparins extracted from animal tissues. The present work provides a detailed study on the structural variants of the tetrasaccharide fragments of this binding site afforded following treatment of a heparin with heparin lyase II. The 5 most commonly observed tetrasaccharide fragments of the AT-binding site are fully characterized, and a method for their quantification in heparin and low-molecular-weight heparin products is described.;
    Description
    Journal of Pharmaceutical Sciences, 106, 973-981; 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
    Elsevier
    Relationships
    The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Journal of Pharmaceutical Sciences; https://harc.rpi.edu/;
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    A full text version is available in DSpace@RPI;
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