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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

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

ASJC Scopus subject areas

  • General


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