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

Data in Brief
Bao Quoc TranYoung Ah Goo

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) [1].

References

May 30, 2012·Biotechnology Progress·P A Marichal-Gallardo, M M Alvarez
Feb 5, 2013·Analytical Chemistry·David P A KilgourPeter B O'Connor

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Citations

Aug 28, 2018·Expert Review of Proteomics·Charlotte GaviardJulie Hardouin
Feb 7, 2019·Critical Reviews in Biotechnology·André GuerraJarka Glassey
Sep 10, 2020·Toxins·Salomé Sauvage, Julie Hardouin

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Methods Mentioned

BETA
electron transfer dissociation
glycosylation

Software Mentioned

Biotools
DataAnalysis
MASH Suite

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