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. 2022 Apr 22;32(8):651–663. doi: 10.1093/glycob/cwac026

Fig. 2.

Fig. 2

Simultaneous nanoLC-qTOF-MS glycopeptide profiling of IgG and IgA. A) Extracted ion chromatograms for the most abundant glycopeptide per glycosylation site (SES-H4N5F1S1, IgG1-H4N4F1, IgG4-H3N4F1, TPL-H5N5F1S1, IgG2/3-H3N4F1, ENI-H5N4S2, HYT-H4N4S1, LAGc-H5N5F1S2, IIV-H5N5F1S2, LAGy-H5N5F1S2, and LSL-H5N4S1). Protein names and the first three letters of the amino acid sequence of the respective tryptic peptide are given (Momcilovic et al. 2020). Separation was based on the peptide backbones, clustering the analytes with the same peptide sequence but varying glycan portions. The blue and orange boxes indicate the time windows used to generate summed spectra in B) and C), respectively. B) The 10 most abundant glycopeptides from the IgA1 HYT O-glycopeptide cluster, with their accurate mass and suggested monosaccharide compositions. C) The 10 most abundant glycopeptides from the IgA1/2 LSL N-glycopeptide cluster, with their accurate mass and proposed N-glycan structures (based on tandem MS and literature). *Signals not derived from glycopeptides. This figure is adjusted with permission from Momcilovic et al. (2020).