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. 2021 Mar 9;11:5505. doi: 10.1038/s41598-021-84771-z

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Linkage analysis of the reaction product. (a) Linkage-specific N-acetylgalactosaminidase digestion of the reaction product. The reaction product purified by SF-HPLC were digested independently by two N-acetylgalactosaminidases specific for α- and β- linkage. The digested products were separated by SF-HPLC. Numbers at the top represent the elution positions of glucose units. (b) Structural representation and fragmentation scheme of GalNAcβ1,4-GlcNAc-pNP. Diagnostic ions are represented in gray characters. (c) Negative ion MS/MS fragmentation spectra of N-acetylgalactosaminylated GlcNAc-pNP. The corresponding m/z values of the CID-derived fragment ions and their nomenclatures are assigned in the spectra. The small window shows the enlarged fragment ions in the mass range m/z 200–500. m/z values shown in black and gray indicate 1,4-linked specific and GalNAcβ-GlcNAc-pNP signals, respectively.