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. 2019 Sep 2;11(8):1381–1390. doi: 10.1080/19420862.2019.1655377

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© 2019 The Author(s). Published with license by Taylor & Francis Group, LLC.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

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Figure 1. — Deuterium uptake curves of glycopeptides (YVDGVEVHNAKTKPREEQYN*STYRVVSVL) containing different glycoforms in human-derived (a) and CHO-expressed (b) IgG1. Data is not corrected for deuterium back exchange. Sialylated glycopeptides are found to have faster H/D exchange rate than other complex glycans in CHO-expressed IgG1, but not human-derived IgG1, indicating that sialylated glycans destabilize the C_H2 domain in CHO-expressed IgG1, but not human-derived IgG1.