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dc.contributor.authorFu, Li
dc.contributor.authorZhang, Fuming
dc.contributor.authorLi, Guoyun
dc.contributor.authorOnishi, Akihiro
dc.contributor.authorBhaskar, Ujjwal
dc.contributor.authorSun, Peilong
dc.contributor.authorLinhardt, Robert J.
dc.date2014
dc.date.accessioned2022-06-23T04:17:32Z
dc.date.available2022-06-23T04:17:32Z
dc.date.issued2014-01-01
dc.identifier.citationStructure and activity of a new low molecular weight heparin produced by enzymatic ultrafiltration, L. Fu, F. Zhang, G. Li, A. Onishi, U. Bhaskar, P. Sun, R. J. Linhardt, Journal of Pharmaceutical Sciences, 103, 1375–1383, 2014.
dc.identifier.issn15206017
dc.identifier.issn223549
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5325
dc.identifier.urihttps://doi.org/10.1002/jps.23939
dc.descriptionJournal of Pharmaceutical Sciences, 103, 1375–1383
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 standard process for preparing the low-molecular-weight heparin (LMWH) tinzaparin, through the partial enzymatic depolymerization of heparin, results in a reduced yield because of the formation of a high content of undesired disaccharides and tetrasaccharides. An enzymatic ultrafiltration reactor for LMWH preparation was developed to overcome this problem. The behavior, of the heparin oligosaccharides and polysaccharides using various membranes and conditions, was investigated to optimize this reactor. A novel product, LMWH-II, was produced from the controlled depolymerization of heparin using heparin lyase II in this optimized ultrafiltration reactor. Enzymatic ultrafiltration provides easy control and high yields (>80%) of LMWH-II. The molecular weight properties of LMWH-II were similar to other commercial LMWHs. The structure of LMWH-II closely matched heparin's core structural features. Most of the common process artifacts, present in many commercial LWMHs, were eliminated as demonstrated by 1D and 2D nuclear magnetic resonance spectroscopy. The antithrombin III and platelet factor-4 binding affinity of LMWH-II were comparable to commercial LMWHs, as was its in vitro anticoagulant activity.
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.titleStructure and activity of a new low molecular weight heparin produced by enzymatic ultrafiltration
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1002/jps.23939
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.pages1375-1383
rpi.description.volume103


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