Show simple item record

dc.contributor.authorChen, Yin
dc.contributor.authorLin, Lei
dc.contributor.authorAgyekum, Isaac
dc.contributor.authorZhang, Xing
dc.contributor.authorSt. Ange, Kalib
dc.contributor.authorYu, Yanlei
dc.contributor.authorZhang, Fuming
dc.contributor.authorLiu, Jian
dc.contributor.authorAmster, I. Jonathan
dc.contributor.authorLinhardt, Robert J.
dc.date2017
dc.date.accessioned2022-06-23T04:28:44Z
dc.date.available2022-06-23T04:28:44Z
dc.date.issued2017-04-01
dc.identifier.citationStructural Analysis of Heparin-Derived 3-O-Sulfated Tetrasaccharides: Antithrombin Binding Site Variants, Y. Chen, L. Lin, I. Agyekum, X. Zhang, K. St.Ange, Y. Yu, J. Liu, I. J. Amster, R. J. Linhardt, Journal of Pharmaceutical Sciences, 106, 973-981, 2017.
dc.identifier.issn15206017
dc.identifier.issn223549
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5387
dc.identifier.urihttps://doi.org/10.1016/j.xphs.2016.11.023
dc.descriptionJournal of Pharmaceutical Sciences, 106, 973-981
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.abstractHeparin is a polysaccharide that is widely used as an anticoagulant drug. The mechanism for heparin's anticoagulant activity is primarily through its interaction with a serine protease inhibitor, antithrombin III (AT), that enhances its ability to inactivate blood coagulation serine proteases, including thrombin (factor IIa) and factor Xa. The AT-binding site in the heparin is one of the most well-studied carbohydrate-protein binding sites and its structure is the basis for the synthesis of the heparin pentasaccharide drug, fondaparinux. Despite our understanding of the structural requirements for the heparin pentasaccharide AT-binding site, there is a lack of data on the natural variability of these binding sites in heparins extracted from animal tissues. The present work provides a detailed study on the structural variants of the tetrasaccharide fragments of this binding site afforded following treatment of a heparin with heparin lyase II. The 5 most commonly observed tetrasaccharide fragments of the AT-binding site are fully characterized, and a method for their quantification in heparin and low-molecular-weight heparin products is described.
dc.description.sponsorshipNational Institutes of Health
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.ispartofJournal of Pharmaceutical Sciences
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleStructural Analysis of Heparin-Derived 3-O-Sulfated Tetrasaccharides: Antithrombin Binding Site Variants
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1016/j.xphs.2016.11.023
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.pages973-981
rpi.description.volume106


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record