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Fig. 1 (abstract O-020). | BMC Proceedings

Fig. 1 (abstract O-020).

From: Abstracts from the 25th European Society for Animal Cell Technology Meeting: Cell Technologies for Innovative Therapies

Fig. 1 (abstract O-020).

a Lectin binding profiles of different IgGs. b Distinction between Fc and Fab glycosylation in Erbitux. c Lectin binding rates correlate with the levels of galactosylation and fucosylation. a Lectin binding profiles of different therapeutic IgGs Arzerra, Mabthera and Avastin solutions of 200 μg/mL in CHO-K1 cell culture supernatant were denatured and the IgG glycans were characterized using nine different lectins. The lectin binding profiles match well with the glycan profiles reported in the literature. b Distinction between Fc and Fab glycosylation in Erbitux. Erbitux was diluted to a concentration of 200 μg/mL in TRIS buffer and measured in native and denatured conditions to distinguish Fab glycosylation (native Erbitux) from Fab and Fc glycosylation (denatured Erbitux). It could be confirmed that sialic acids are almost exclusively present on the Fab part of Erbitux and that the high mannose glycans are only found in the Fc part. c Lectin binding rates correlate with the levels of galactosylation and fucosylation. Two glycan variants samples of the same IgG from Merck were mixed in different ratios to yield glycosylation rates of 9 to 55% in terminal β-galactose and 8 to 100% in core-fucose, based on data from 2-AB UPLC analysis. The mixtures all contained 0.5 μg IgG per well. The measured lectin binding rates for all galactose and fucose markers correlate very well with the respective degree of glycosylation in the mixtures. All measurements were performed in triplicates

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