Heparin stability by determining unsubstituted amino groups using HILIC-MS

Authors
Fu, L.
Li, L.
Cai, C.
Li, G.
Zhang, F.
Linhardt, Robert J.
ORCID
https://orcid.org/0000-0003-2219-5833
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Issue Date
2014
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
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Full Citation
Heparin stability by determining unsubstituted amino groups using HILIC-MS, L. Fu, L. Li, C. Cai, G. Li, F. Zhang, Robert J. Linhardt, Analytical Biochemistry, 461, 46–48, 2014.
Abstract
The thermal instability of the anticoagulant heparin is associated, in part, with the solvolytic loss of N-sulfo groups. This study describes a new method to assess the increased content of unsubstituted amino groups present in thermally-stressed and autoclave-sterilized heparin formulations. N-acetylation of heparin samples with acetic anhydride-d6 is followed by exhaustive heparinase treatment, and disaccharide analysis by hydrophilic interaction chromatography mass spectrometry. The introduction of stable isotopic label provides a sensitive probe for the detection and localization of the lost N-sulfo groups potentially providing valuable insights into degradation mechanism and the reasons for anticoagulant potency loss.
Description
Analytical Biochemistry, 461, 46–48
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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
https://harc.rpi.edu/
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A full text version is available in DSpace@RPI