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dc.contributor.authorLeBrun, L.A.
dc.contributor.authorLinhardt, Robert J.
dc.date2001
dc.date.accessioned2022-06-27T16:20:26Z
dc.date.available2022-06-27T16:20:26Z
dc.date.issued2001-01-01
dc.identifier.citationDegradation of Heparan Sulfate with Heparin Lyases, L.A. LeBrun, R.J. Linhardt, in Methods in Molecular Biology, Proteoglycan Protocols: Current Methods and Applications, Vol. 171, R.V. Iozzo, ed., Humana Press, Totowa, NJ, Chap. 35, pp 353-361, 2001.
dc.identifier.issn10643745
dc.identifier.urihttps://doi.org/10.1385/1-59259-209-0:353
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5857
dc.descriptionin Methods in Molecular Biology, Proteoglycan Protocols: Current Methods and Applications, Vol. 171, R.V. Iozzo, ed., Humana Press, Totowa, NJ, Chap. 35, pp 353-361
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.abstractGlycosaminoglycan (GAG), heparan sulfate (HS), and heparin are a polydisperse mixture of linear polysaccharides composed of glucosamine residues 1→ 4 linked to uronic acid residues. The major repeating unit in heparin is → 4)-α-D-N-sulfoglucosamine-6-sulfate (1? 4)-α-L-iduronic acid-2-sulfate (1?, corresponds to 75-90% of its sequence (1) (see Fig. 1A), whereas heparan sulfate consists of 50-75% ? 4)α-D-N-acetylglucosamine (1? 4)-β-glucuronic acid (1? and smaller amounts of → 4)-α-D-N-acetylglucosamine-6-sulfate (1? 4)-β-D-glucuronic acid (1? and ? 4)α-D-N-sulfoglucosamine (1? 4)-β-D-glucuronic acid (1? (see Fig. 1B). Heparin, which contains approx 2.7 sulfate groups per disaccharide unit, is more highly sulfated than HS, which contains less than one sulfate per disaccharide unit.
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1385/1-59259-209-0:353
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofMethods in molecular biology (Clifton, N.J.)
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleDegradation of Heparan Sulfate with Heparin Lyases
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1385/1-59259-209-0:353
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dcterms.isVersionOfhttps://doi.org/10.1385/1-59259-209-0:353
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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.pages353-361
rpi.description.volume171


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