cancel
Showing results for 
Search instead for 
Did you mean: 

Structural Characterization of 150 kDa Intact Antibodies with Electron Transfer Dissociation Orbitrap Mass Spectrometry

Orbitrap_SciLib
Reputable Mentor II
Reputable Mentor II
Tsybin Y, Damoc E, Fornelli L, Miladinovic S, Nolting D, Zeller M, Grouzmann E, Makarov A.
ASMS 2011 Poster
• ETD on Orbitrap FTMS produced 162 identified unique backbone cleavages sites on ~150 kDa intact protein (IgG) on the LC timescale. • Sequence coverage obtained by ETD is generally higher than the one obtained by slow-heating activation methods and, importantly, provides valuable information on the variable domains. • ETD fragmentation patterns of IgGs derived from different organisms (i. e., with significant differences in sequence-structure) show relevant differences in the number and abundances of product ions, especially in the 200-1200 m/z region. • Further improvement in S/N is required for identification of PTMs and increased sequence coverage.


Ecole Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.
Version history
Last update:
‎10-15-2021 12:07 PM
Updated by:
AnalyteGuru
Contributors