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    Sequence Analysis of Highly Sulfated Heparin-Derived Oligosaccharides Using Fast Atom Bombardment Mass Spectrometry

    Author
    Mallis, Larry M.; Wang, Hui M.; Loganathan, Duraikkannu; Linhardt, Robert J.
    ORCID
    https://orcid.org/0000-0003-2219-5833
    Thumbnail
    Other Contributors
    Date Issued
    1989-01-01
    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
    Sequence Analysis of Highly Sulfated Heparin-Derived Oligosaccharides Using Fast Atom Bombardment Mass Spectrometry, L.M. Mallis, H.M. Wang, D. Loganathan, R.J. Linhardt, Analytical Chemistry, 61, 1453-1458 (1989).
    Metadata
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    URI
    https://doi.org/10.1021/ac00188a030; https://hdl.handle.net/20.500.13015/6011
    Abstract
    Heparin, a polydisperse, sulfated copolymer of 1----4 linked glucosamine and uronic acid residues, has been used clinically as an anticoagulant for half a century. Despite a yearly use of over 50 million doses in the U.S. alone, heparin's exact chemical structure remains unclear. The negative ion fast atom bombardment mass spectrometry (FAB-MS) analysis is presented for a series of enzymatically prepared, homogeneous, structurally characterized, highly sulfated, heparin-derived oligosaccharides using triethanolamine as the FAB matrix. In addition to the clear presence of monoanionic sodiated molecular ions, structurally significant (sequence) fragment ions are observed and characterized with respect to the known structure for five of the heparin-derived oligosaccharides. The structure of a sixth oligosaccharide is predicted by using negative ion FAB-MS and subsequently confirmed by chemical, enzymatic, and NMR spectroscopic methods.;
    Description
    Analytical Chemistry, 61, 1453-1458; 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; Analytical Chemistry; https://harc.rpi.edu/;
    Access
    https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1021/ac00188a030;
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