Epitope mapping of 7S cashew antigen in complex with antibody by solution‐phase H/D exchange monitored by FT‐ICR mass spectrometry
Journal of Mass Spectrometry, 2015•Wiley Online Library
The potential epitope of a recombinant food allergen protein, cashew Ana o 1, reactive to
monoclonal antibody, mAb 2G4, has been mapped by solution‐phase amide backbone H/D
exchange (HDX) monitored by Fourier transform ion cyclotron resonance mass spectrometry
(FT‐ICR MS). Purified mAb 2G4 was incubated with recombinant Ana o 1 (rAna o 1) to form
antigen: monoclonal antibody (Ag: mAb) complexes. Complexed and uncomplexed (free)
rAna o 1 were then subjected to HDX‐MS analysis. Five regions protected from H/D …
monoclonal antibody, mAb 2G4, has been mapped by solution‐phase amide backbone H/D
exchange (HDX) monitored by Fourier transform ion cyclotron resonance mass spectrometry
(FT‐ICR MS). Purified mAb 2G4 was incubated with recombinant Ana o 1 (rAna o 1) to form
antigen: monoclonal antibody (Ag: mAb) complexes. Complexed and uncomplexed (free)
rAna o 1 were then subjected to HDX‐MS analysis. Five regions protected from H/D …
The potential epitope of a recombinant food allergen protein, cashew Ana o 1, reactive to monoclonal antibody, mAb 2G4, has been mapped by solution‐phase amide backbone H/D exchange (HDX) monitored by Fourier transform ion cyclotron resonance mass spectrometry (FT‐ICR MS). Purified mAb 2G4 was incubated with recombinant Ana o 1 (rAna o 1) to form antigen:monoclonal antibody (Ag:mAb) complexes. Complexed and uncomplexed (free) rAna o 1 were then subjected to HDX‐MS analysis. Five regions protected from H/D exchange upon mAb binding are identified as potential conformational epitope‐contributing segments. Copyright © 2015 John Wiley & Sons, Ltd.
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