Glycosylation characterization of therapeutic mAbs by top- and middle-down mass spectrometry

Bao Quoc Tran, Christopher Barton, Jinhua Feng, Aimee Sandjong, Sung Hwan Yoon, Shivangi Awasthi, Tao Liang, Mohd M. Khan, David P.A. Kilgour, David R. Goodlett, Young Ah Goo

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


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].

Original languageEnglish
Pages (from-to)68-76
Number of pages9
JournalData in Brief
StatePublished - Mar 1 2016


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