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    Analysis of the glycosaminoglycan chains of proteoglycans

    Author
    Song, Yuefan; Zhang, Fuming; Linhardt, Robert J.
    ORCID
    https://orcid.org/0000-0003-2219-5833
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    ANALYSIS OF THE GLYCOSAMINOGLYCAN CHAINS OF PROTEOGLYCANS.pdf (1.372Mb)
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    Date Issued
    2021-02-01
    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
    Analysis of the glycosaminoglycan chains of proteoglycans, Y. Song, F. Zhang, R. J. Linhardt, Journal of Histochemistry & Cytochemistry, 69, 121 –135, 2021.
    Metadata
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    URI
    https://hdl.handle.net/20.500.13015/5409; https://doi.org/10.1369/0022155420937154
    Abstract
    Glycosaminoglycans (GAGs) are heterogeneous, negatively charged, macromolecules that are found in animal tissues. Based on the form of component sugar, GAGs have been categorized into four different families: heparin/heparan sulfate, chondroitin/dermatan sulfate, keratan sulfate, and hyaluronan. GAGs engage in biological pathway regulation through their interaction with protein ligands. Detailed structural information on GAG chains is required to further understanding of GAG–ligand interactions. However, polysaccharide sequencing has lagged behind protein and DNA sequencing due to the non-template-driven biosynthesis of glycans. In this review, we summarize recent progress in the analysis of GAG chains, specifically focusing on techniques related to mass spectroscopy (MS), including separation techniques coupled to MS, tandem MS, and bioinformatics software for MS spectrum interpretation. Progress in the use of other structural analysis tools, such as nuclear magnetic resonance (NMR) and hyphenated techniques, is included to provide a comprehensive perspective.;
    Description
    Journal of Histochemistry & Cytochemistry, 69, 121 –135; 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
    Sage
    Relationships
    The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Journal of Histochemistry and Cytochemistry; https://harc.rpi.edu/;
    Access
    Open Access; A full text version is available in DSpace@RPI;
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