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    Enzymatic Redesigning of Biological Active Heparan Sulfate

    Author
    Chen, J.; Avci, F.Y.; Muñoz, E.M.; McDowell, L.M.; Chen, M.; Pedersen, L.C.; Zhang, L.; Linhardt, Robert J.; Liu, J.
    ORCID
    https://orcid.org/0000-0003-2219-5833
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    ENZYMATIC REDESIGNING OF BIOLOGICALLY ACTIVE HEPARAN SULFATE.pdf (797.9Kb)
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    Date Issued
    2005
    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
    Enzymatic Redesigning of Biological Active Heparan Sulfate, J. Chen, F.Y. Avci, E. M. Muñoz, L. M. McDowell, M. Chen, L. C. Pedersen, L. Zhang, R. J. Linhardt, J. Liu, Journal of Biological Chemistry, 280, 42817-42825, 2005.
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    URI
    https://hdl.handle.net/20.500.13015/5185; https://doi.org/10.1074/jbc.M504338200
    Abstract
    Heparan sulfate carries a wide range of biological activities, regulating blood coagulation, cell differentiation, and inflammatory responses. The sulfation patterns of the polysaccharide are essential for the biological activities. In this study, we report an enzymatic method for the sulfation of multimilligram amounts of heparan sulfate with specific functions using immobilized sulfotransferases combined with a 3′-phosphoadenosine 5′-phosphosulfate regeneration system. By selecting appropriate enzymatic modification steps, an inactive precursor has been converted to the heparan sulfate having three distinct biological activities, associated with binding to antithrombin, fibroblast growth factor-2, and herpes simplex virus envelope glycoprotein D. Because the recombinant sulfotransferases are expressed in bacteria, and the method uses a low cost sulfo donor, it can be readily utilized to synthesize large quantities of anticoagulant heparin drug or other biologically active heparan sulfates.;
    Description
    Journal of Biological Chemistry, 280, 42817-42825; 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; https://harc.rpi.edu/;
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    A full text version is available in DSpace@RPI;
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