Heparin stability by determining unsubstituted amino groups using HILIC-MS

Fu, L.
Li, L.
Cai, C.
Li, G.
Zhang, F.
Linhardt, Robert J.
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Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
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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.
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.
Analytical Biochemistry, 461, 46–48
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The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
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