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. 2016 Nov 21;28(2):229–241. doi: 10.1007/s13361-016-1539-1

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© The Author(s) 2016

Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

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Oxonium ion analysis of protonated CS-glycopeptides originating from the monosulfated glycoform. (a) HCD spectrum of the m/z 100–400 region showing the oxonium ions. (b) CID-MS3 of the [ΔHexAGalNAc]⁺ ion at m/z 362.11. (c) HCD spectrum at the m/z 100–400 region for the mono-sulfated glycoform containing an intact terminal GlcA residue. (d) Proposed decomposition pathways for the m/z 362.11 and 380.12 (red) ions. All major oxonium ions are annotated with glycan structures and ions marked with * are specified in Table 2. HCD and CID were performed at a NCE of 30%