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dc.contributor.authorBeaudet, Julie M.
dc.contributor.authorWeyers, Amanda
dc.contributor.authorSolakyildirim, Kemal
dc.contributor.authorYang, Bo
dc.contributor.authorTakieddin, Majde
dc.contributor.authorMousa, Shaker
dc.contributor.authorZhang, Fuming
dc.contributor.authorLinhardt, Robert J.
dc.date2011
dc.date.accessioned2022-06-23T04:11:28Z
dc.date.available2022-06-23T04:11:28Z
dc.date.issued2011-01-01
dc.identifier.citationImpact of autoclave sterilization on the activity and structure of formulated heparin, J. M. Beaudet, A. Weyers, K. Solakyildirim, B. Yang, M. Takieddin, S. Mousa, F. Zhang, R. J. Linhardt, Journal of Pharmaceutical Science, 100, 3396–3404, 2011.
dc.identifier.issn15206017
dc.identifier.issn223549
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5287
dc.identifier.urihttps://doi.org/10.1002/jps.22527
dc.descriptionJournal of Pharmaceutical Science, 100, 3396–3404
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 stability of a formulated heparin was examined during its sterilization by autoclaving. A new method to follow loss in heparin binding to the serine protease inhibitor, antithrombin III, and the serine protease, thrombin, was developed using a surface plasmon resonance competitive binding assay. This loss in binding affinity correlated well with loss in antifactor IIa (thrombin) activity as well as antifactor Xa activity as measured using conventional amidolytic assays. Autoclaving also resulted in a modest breakdown of the heparin backbone as confirmed by a slight reduction in number-averaged and weight-averaged molecular weight and an increase in polydispersity. Although no clear changes were observed by nuclear magnetic resonance spectroscopy, disaccharide composition analysis using high-performance liquid chromatography-electrospray ionization-mass spectrometry suggested that loss of selected sulfo groups had taken place. It is this sulfo group loss that probably accounts for a decrease in the binding of autoclaved heparin to antithrombin III and thrombin as well as the observed decrease in its amidolytic 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.titleImpact of autoclave sterilization on the activity and structure of formulated heparin
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1002/jps.22527
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.pages3396-3404
rpi.description.volume100


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