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Updated: Aug 8, 2025

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Published on: June 21, 2021
Characterization of antithrombin isoforms and latent forms by ion exchange chromatography coupled to mass
Yann Leblanc1, Violaine Chapuis1, Valegh Faid1
1Analytical Department of LFB Biotechnologies, 3 Avenue des Tropiques, 91958, Courtabœuf, France.
Abstract:
Antithrombin is a key protein of the coagulation system belonging to the serine protease inhibitor family. Antithrombin preparations are used as a therapeutic treatment for patients with decreased antithrombin activity. Elucidating the structural features of this protein is an important part of the control strategy to assure a high quality. This study presents an ion exchange chromatographic method coupled to mass spectrometry capable of characterizing antithrombin post-translational modifications such as N-glycosylation, phosphorylation or deamidation. Furthermore, the method was successfully used to evidence irreversible/inactive conformers of antithrombin which are commonly observed for serine protease inhibitors and referred to as latent forms.
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