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. 2015 Apr 15;7(3):571–583. doi: 10.1080/19420862.2015.1029215

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© 2015 The Author(s). Published with license by Taylor & Francis Group, LLC

© 2015 Crown copyright

This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

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Figure 2. — Lectin-blot analyses of TZM from culture supernatants. Various amounts of glycosyltransferases and harvest time were tested for optimal galactosylation and sialylation of the Fc. The lectin-blots show the mAbs’ heavy chain (reducing gels). Ponceau red staining was used to control the protein load. Panel (A) Co-expression of TZM and GT. The DNA mix was composed of 0% to 10% in weight of GT encoding plasmid, the rest being a 6:4 mixture of plasmids coding for TZM light and heavy chains. ECL was used to detect terminal galactosylation. Panel (B) Co-expression of TZM, GT and ST6. The DNA mix was composed of 2% of GT plasmid with 0% to 20% of ST6 coding plasmid, the rest being a 6:4 mixture of plasmids coding for TZM light and heavy chains. SNA was used to detect terminal α2,6-sialylation. Panel (C) HC α2,6-sialylation level from day 2 to day 9 post-transfection.