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

Tran, B.Q., Barton, C., Feng, J., Sandjong, A., Yoon, S.H., Awasthi, S., Liang, T., Khan, M.M., Kilgour, D.P.A. ORCID: 0000-0002-3860-7532, Goodlett, D.R. and Goo, Y.A., 2016. Glycosylation characterization of therapeutic mAbs by top- and middle-down mass spectrometry. Data in Brief, 6, pp. 68-76. ISSN 2352-3409

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Abstract

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).

Item Type: Journal article
Publication Title: Data in Brief
Creators: Tran, B.Q., Barton, C., Feng, J., Sandjong, A., Yoon, S.H., Awasthi, S., Liang, T., Khan, M.M., Kilgour, D.P.A., Goodlett, D.R. and Goo, Y.A.
Publisher: Elsevier
Date: March 2016
Volume: 6
ISSN: 2352-3409
Identifiers:
NumberType
10.1016/j.dib.2015.11.031DOI
Divisions: Schools > School of Science and Technology
Depositing User: Jill Tomkinson
Date Added: 30 Jun 2016 15:21
Last Modified: 09 Jun 2017 14:03
URI: http://irep.ntu.ac.uk/id/eprint/28026

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