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dc.contributor.authorYan, Lufeng
dc.contributor.authorBrodfueher, Paul
dc.contributor.authorFu, Li
dc.contributor.authorZhang, Fuming
dc.contributor.authorChen, Shiguo
dc.contributor.authorDordick, Jonathan S.
dc.contributor.authorLinhardt, Robert J.
dc.date2020
dc.date.accessioned2022-06-27T15:40:48Z
dc.date.available2022-06-27T15:40:48Z
dc.date.issued2020-10-01
dc.identifier.citationChemical O-sulfation of N-sulfoheparosan: A route to rare N-sulfo-3-O-sulfoglucosamine and 2-O-sulfoglucuronic acid, L. Yan, P. Brodfueher, L. Fu, F. Zhang, S. Chen, J. S. Dordick, R. J. Linhardt, Glycoconjugate Journal, 37, 589–597, 2020.
dc.identifier.issn15734986
dc.identifier.issn2820080
dc.identifier.urihttps://doi.org/10.1007/s10719-020-09939-7
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5482
dc.descriptionGlycoconjugate Journal, 37, 589–597
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.abstractHeparosan, the capsular polysaccharide of E. coli K5 is currently used as the starting material in the chemoenzymatic synthesis of heparan sulfate and the structurally related anticoagulant drug heparin. Base hydrolysis of N-acetyl groups and their subsequent N-sulfonation, are used to prepare N-sulfoheparosan an intermediate of biosynthesis. In the present study, when excess sulfonation reagent was used during N-sulfonation, some O-sulfation also took place in the N-sulfoheparosan product. After a nearly full digestion, a hexasaccharide fraction exhibited resistance to heparin lyase II. Excessive digestion by heparin lyase II and structural identification by NMR and mass spectroscopy indicated that the resistant hexasaccharide fraction has two structures, ΔUA-GlcNS-GlcA2S-GlcNS-GlcA-GlcNS and ΔUA-GlcNS-GlcA- GlcNS3S-GlcA-GlcNS in similar amounts. The 2-sulfated structure exhibited partial resistance to heparin lyase II; however the structure of ΔUA-GlcNS-GlcA-GlcNS3S was completely resistant to heparin lyase II.
dc.description.sponsorshipNational Institutes of Health
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1007/s10719-020-09939-7
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofGlycoconjugate Journal
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleChemical O-sulfation of N-sulfoheparosan: A route to rare N-sulfo-3-O-sulfoglucosamine and 2-O-sulfoglucuronic acid
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1007/s10719-020-09939-7
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1007/s10719-020-09939-7
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)
rpi.description.pages589-597
rpi.description.volume37


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