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. 2019 Dec 17;9:19242. doi: 10.1038/s41598-019-55805-4

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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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(a) SDS-PAGE of purified Abs using a 4–20% gradient polyacrylamide gel. (b) Glycosylation analysis. MC-6C407 and MC-3D8 IgY proteins, treated with or without a mixture of glycosylases, were separated by SDS-PAGE followed by Coomassie Blue staining (upper panel) or PAS staining (lower panel). F, fetuin (64 kDa control for deglycosylation conditions); P, horseradish peroxidase (44 kDa positive control for glycoprotein staining); N, soybean trypsin inhibitor (20 kDa negative control for glycoprotein staining).