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dc.contributor.authorHileman, Ronald E.
dc.contributor.authorSmith, April E.
dc.contributor.authorToida, Toshihiko
dc.contributor.authorLinhardt, Robert J.
dc.date1997
dc.date.accessioned2022-06-27T17:13:19Z
dc.date.available2022-06-27T17:13:19Z
dc.date.issued1997-03-01
dc.identifier.citationPreparation and Structure of Heparin Lyase-Derived Heparan SulphateOligosaccharides, R. E. Hileman, T. Toida, A. E. Smith, R.J. Linhardt,Glycobiology,7,231-239, 1997.
dc.identifier.issn9596658
dc.identifier.urihttps://doi.org/10.1093/glycob/7.2.231
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5930
dc.descriptionGlycobiology, 7, 231-239
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.abstractPorcine intestinal mucosal heparan sulfate was exhaustively depolymerized on a large scale using beparin lyase II (heparinase II) or heparin lyase III (heparitinase, EC 4.2.2.8). The oligosaccharide mixtures formed with each enzyme were fractionated by low pressure gel permeation chromatography. Size-uniform mixtures of disaccharides, tetrasaccharides, and hexasaccharides were obtained. Each size-fractionated mixture was then purified on the basis of charge by repetitive semipreparative strong-anion-exchange high-performance liquid chromatography. This approach has led to the isolation of 13 homogenous oligosaccharides. The purity of each oligosaccharide was demonstrated by the presence of a single peak on analytical strong-anion-exchange high-performance liquid chromatography and reversed polarity capillary electrophoresis. The structures of these oligosaccharides were established using 500 MHz one- and two-dimensional nuclear magnetic resonance spectroscopy. Three of the thirteen structures that were solved were novel while the remaining 10 have been previously described. All of the structures obtained using heparin lyase III contained a ΔUAp residue (where ΔUAp is 4-deoxy-α-L-threo-hex-4-eno-pyranosyluronic acid) at their nonreducing termini. Structures obtained using heparin lyase II contained both ΔUAp and ΔUAp2S (where S is sulfate) at their nonreducing termini. These results are consistent with the reported specificity of both enzymes.
dc.description.sponsorshipNational Institutes of Health
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1093/glycob/7.2.231
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofGlycobiology
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titlePreparation and Structure of Heparin Lyase-Derived Heparan Sulphate Oligosaccharides
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1093/glycob/7.2.231
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dcterms.isVersionOfhttps://doi.org/10.1093/glycob/7.2.231
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.pages231-239
rpi.description.volume7


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