Glycosylation characterization of therapeutic mAbs by top- and middle-down mass spectrometry
2016
Tran, Bao Quoc | Barton, Christopher | Feng, Jinhua | Sandjong, Aimee | Yoon, Sung Hwan | Awasthi, Shivangi | Liang, Tao | Khan, Mohd M. | Kilgour, David P.A. | Goodlett, David R. | Goo, Young Ah
A reference monoclonal antibody IgG1 and a fusion IgG protein were analyzed by top- and middle-down mass spectrometry with multiple fragmentation techniques including electron transfer dissociation (ETD) and matrix-assisted laser desorption ionization in-source decay (MALDI-ISD) to investigate heterogeneity of glycosylated protein species. Specifically, glycan structure, sites, relative abundance levels, and termini structural conformation were investigated by use of Fourier transform ion cyclotron resonance (FT-ICR) or high performance liquid chromatography electrospray ionization (HPLC-ESI) linked to an Orbitrap. Incorporating a limited enzymatic digestion by immunoglobulin G-degrading enzyme Streptococcus pyogenes (IdeS) with MALDI-ISD analysis extended sequence coverage of the internal region of the proteins without pre-fractionation. The data in this article is associated with the research article published in Journal of Proteomics (Tran et al., 2015) [1].
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