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. 2019 Jul 26;11(6):1053–1063. doi: 10.1080/19420862.2019.1630218

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© 2019 The Author(s). Published with license by Taylor & Francis Group, LLC.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

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Figure 3. — MS/MS spectra of pronase-treated O-glycopeptides of atacicept. (a) Stepping-energy CID spectra of the O-glycopeptide ₈₆SDKT₈₉ covering glycosylation site Ser86 with a monosialylated core 1-type glycan. (b) Stepping-energy CID spectra of the O-glycopeptide ₉₁TCPPCPAPE₉₉ covering the glycosylation site Thr91 with a monosialylated core 1-type glycan. (c + d) ETD spectra of the O-glycopeptide ₈₆SDKT₈₉ covering glycosylation site Ser86 carrying a monosialylated core 1-type glycan from two different production batches. Compounds with the same mass and retention time from two different production batches were compared featuring the same fragmentation pattern and thus, could be identified as the same glycopeptides.