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Heparin stability by determining unsubstituted amino groups using hydrophilic interaction chromatography mass spectrometry.


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 (HILIC-MS). The introduction of a stable isotopic label provides a sensitive probe for the detection and localization of the lost N-sulfo groups, potentially providing valuable insights into the degradation mechanism and the reasons for anticoagulant potency loss.

SUBMITTER: Fu L 

PROVIDER: S-EPMC4119833 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature

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Heparin stability by determining unsubstituted amino groups using hydrophilic interaction chromatography mass spectrometry.

Fu Li L   Li Lingyun L   Cai Chao C   Li Guoyun G   Zhang Fuming F   Linhardt Robert J RJ  

Analytical biochemistry 20140606


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 (HILIC-MS). The  ...[more]

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