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dc.contributor.authorChen, J.
dc.contributor.authorAvci, F.Y.
dc.contributor.authorMuñoz, E.M.
dc.contributor.authorMcDowell, L.M.
dc.contributor.authorChen, M.
dc.contributor.authorPedersen, L.C.
dc.contributor.authorZhang, L.
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorLiu, J.
dc.date2005
dc.date.accessioned2022-06-23T03:56:10Z
dc.date.available2022-06-23T03:56:10Z
dc.date.issued2005
dc.identifier.citationEnzymatic 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.
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5185
dc.identifier.urihttps://doi.org/10.1074/jbc.M504338200
dc.descriptionJournal of Biological Chemistry, 280, 42817-42825
dc.descriptionNote : 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.
dc.description.abstractHeparan 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.
dc.languageen_US
dc.language.isoENG
dc.publisherElsevier
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleEnzymatic Redesigning of Biological Active Heparan Sulfate
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isVersionOfhttps://doi.org/10.1074/jbc.M504338200
dc.rights.holderIn 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/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)


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