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. 2020 Oct 16;37(6):691–702. doi: 10.1007/s10719-020-09953-9

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© The Author(s) 2020

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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Fig. 4 — Confirmation of complete de-galactosylation of terminal galactose residues of N-glycans on IgG glycoproteins by the exoglycosidase treatment in the glycosidase plate-based assay. The released N-glycans from IgG glycoproteins (a) without galactosidase treatment was compared with (b) galactosidase treatment on a HILIC-FLD-MSn platform after labelling the reducing end with procainamide. For the confirmation of complete de-galactosylation and de-sialylation of N-glycans on IgG glycoproteins please see supplementary fig. S6. [Proc: procainamide; Blue square: N-acetylglucosamine, green circle: mannose, yellow circle: galactose, white circle: ambiguous hexose, red triangle: fucose, pink diamond: N-acetylneuraminic acid]