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    Impact of autoclave sterilization on the activity and structure of formulated heparin

    Author
    Beaudet, Julie M.; Weyers, Amanda; Solakyildirim, Kemal; Yang, Bo; Takieddin, Majde; Mousa, Shaker; Zhang, Fuming; Linhardt, Robert J.
    ORCID
    https://orcid.org/0000-0003-2219-5833
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    IMPACT OF AUTOCLAVE STERILIZATION ON THE ACTIVITY AND STRUCTURE OF.pdf (835.7Kb)
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    Date Issued
    2011-01-01
    Subject
    Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
    Degree
    Terms of Use
    In 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/;
    Full Citation
    Impact 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.
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    URI
    https://hdl.handle.net/20.500.13015/5287; https://doi.org/10.1002/jps.22527
    Abstract
    The 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.;
    Description
    Journal of Pharmaceutical Science, 100, 3396–3404; Note : 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.
    Department
    The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
    Publisher
    Elsevier
    Relationships
    The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Journal of Pharmaceutical Sciences; https://harc.rpi.edu/;
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    A full text version is available in DSpace@RPI;
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