Show simple item record

dc.contributor.authorVongchan, Preeyanat
dc.contributor.authorWarda, Mohamad
dc.contributor.authorToyoda, Hidenao
dc.contributor.authorToida, Toshihiko
dc.contributor.authorMarks, Rory M.
dc.contributor.authorLinhardt, Robert J.
dc.date2005
dc.date.accessioned2022-06-27T16:16:03Z
dc.date.available2022-06-27T16:16:03Z
dc.date.issued2005-01-19
dc.identifier.citationStructural Characterization of Human Liver Heparan Sulfate, P. Vongchan, M. Warda, H. Toyoda, T. Toida, R. M. Marks, R. J. Linhardt, Biochemica Biophysica Acta, 1721, 1-8, 2005.
dc.identifier.issn3044165
dc.identifier.urihttps://doi.org/10.1016/j.bbagen.2004.09.007
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5780
dc.descriptionBiochemica Biophysica Acta, 1721, 1-8
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.abstractThe isolation, purification and structural characterization of human liver heparan sulfate are described. 1H-NMR spectroscopy demonstrates the purity of this glycosaminoglycan (GAG) and two-dimensional 1H-NMR confirmed that it was heparan sulfate. Enzymatic depolymerization of the isolated heparan sulfate, followed by gradient polyacrylamide gel, confirmed its heparin lyase sensitivity. The concentration of resulting unsaturated disaccharides was determined using reverse phase ion-pairing (RPIP) HPLC with post column derivatization and fluorescence detection. The results of this analysis clearly demonstrate that the isolated GAG was heparan sulfate, not heparin. Human liver heparan sulfate was similar to heparin in that it has a reduced content of unsulfated disaccharide and an elevated average sulfation level. The antithrombin-mediated anti-factor Xa activity of human liver heparan sulfate, however, was much lower than porcine intestinal (pharmaceutical) heparin but was comparable to standard porcine intestinal heparan sulfate. Moreover, human liver heparan sulfate shows higher degree of sulfation than heparan sulfate isolated from porcine liver or from the human hepatoma Hep 2G cell line.
dc.description.sponsorshipNational Heart, Lung, and Blood Institute
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/j.bbagen.2004.09.007
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofBiochimica et Biophysica Acta - General Subjects
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleStructural Characterization of Human Liver Heparan Sulfate
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/j.bbagen.2004.09.007
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1016/j.bbagen.2004.09.007
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.pages1-8
rpi.description.volume1721


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record