Field-amplified sample stacking for the detection of chemical warfare agent degradation products in low-conductivity matrices by capillary electrophoresis-mass spectrometry

2008 ◽  
Vol 1178 (1-2) ◽  
pp. 239-247 ◽  
Author(s):  
Mélanie Lagarrigue ◽  
Anne Bossée ◽  
Arlette Bégos ◽  
Nathalie Delaunay ◽  
Anne Varenne ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Capillary Electrophoresis ◽  
Degradation Products ◽  
Chemical Warfare Agent ◽  
Chemical Warfare ◽  
Sample Stacking ◽  
Capillary Electrophoresis Mass Spectrometry

Rapid Screening of Aqueous Chemical Warfare Agent Degradation Products:  Ambient Pressure Ion Mobility Mass Spectrometry

2002 ◽  
Vol 74 (17) ◽  
pp. 4343-4352 ◽  
Author(s):  
Wes E. Steiner ◽  
Brian H. Clowers ◽  
Laura M. Matz ◽  
William F. Siems ◽  
Herbert H. Hill
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Degradation Products ◽  
Ambient Pressure ◽  
Chemical Warfare Agent ◽  
Chemical Warfare ◽  
Rapid Screening ◽  
Ion Mobility Mass Spectrometry

scholarly journals Intact monoclonal antibodies separation and analysis by sheathless capillary electrophoresis-mass spectrometry

2018 ◽  
Vol 25 (3) ◽  
pp. 324-332 ◽  
Author(s):  
Jérémie Giorgetti ◽  
Antony Lechner ◽  
Elise Del Nero ◽  
Alain Beck ◽  
Yannis-Nicolas François ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Capillary Electrophoresis ◽  
Monoclonal Antibodies ◽  
Degradation Products ◽  
Background Electrolyte ◽  
Ease Of Use ◽  
High Mass ◽  
Intact Protein ◽  
Set Up ◽  
Capillary Electrophoresis Mass Spectrometry

Capillary electrophoresis-mass spectrometry coupling is a growing technique in biopharmaceutics characterization. Assessment of monoclonal antibodies is well known at middle-up and bottom-up levels to obtain information about the sequence, post-translational modifications and degradation products. Intact protein analysis is an actual challenge to be closer to the real protein structure. At this level, actual techniques are time consuming or cumbersome processes. In this work, a 20 minutes separation method has been developed to optimize characterization of intact monoclonal antibodies. Thus, separation has been done on a positively charged coated capillary with optimized volatile background electrolyte and sample buffer. Three world-wide health authorities approved monoclonal antibodies have been used to set up a rapid and ease of use method. Intact trastuzumab, rituximab and palivizumab isoforms have been partially separated with this method in less than 20 minutes under denaturing conditions. For each monoclonal antibody, 2X-glycosylated and 1X-glycosylated structures have been identified and separated. Concerning basic and acidic variants, potential aspartic acid isomerization modification and asparagine deamidation have been observed. Accurate mass determination for high-mass molecular species remains a challenge, but the progress in intact monoclonal antibodies separation appears very promising for biopharmaceutics characterization.

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