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. 2019 Apr 17;10(1):87–97. doi: 10.1080/21655979.2019.1604037

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© 2019 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — Biochemical characterization of recombinant AAT-(AP)₂₀ fusion proteins. (a) SDS-PAGE separation of AAT-(AP)₂₀ purified from the culture media. (b) Monosaccharide compositions of the AAT-(AP)₂₀ fusion proteins. The weight percentage (wt %) of each sugar residue accounts for the total fusion protein is presented and the value indicated on the top of each bar. The number in brackets indicates the molar ratio of each sugar residue in the glycans attached to the AAT-(AP)₂₀ polypeptide. Rha, Ara, Gal, and GlcUA are typical sugar residues of Hyp-glycans; GlcNAc, Man, Xyl and Fuc are typical sugar residues of N-glycans.