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. 2019 Apr 30;10:1785. doi: 10.1038/s41467-019-09809-3

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© The Author(s) 2019

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — Site-specific glycan analyses of α-galactosidase A (GLA) glycoforms produced with combinatorial gene engineering of CHO cells. a–l The two most abundant glycan structures at N-glycosites (N108, N161, and N184) of GLA are shown. Each glycan structure was confirmed by targeted tandem mass spectrometry (MS/MS) analysis. The detailed N-glycan analyses of all GLA glycoforms are shown in Supplementary Fig. 2 together with additional variants. Details regarding the stacking ancestry and sequence analysis are shown in Supplementary Table 2 and Supplementary Data 1