Figure 2
N-linked glycosylation stabilizes the VWF A2 domain through the N1574-GlcNAc linkage. DSF measurements, expressed as percent fluorescence (% FU), were carried out in the presence of 1 mM EDTA (open symbols) or 5 mM CaCl2 (closed symbols). WT VWF A2 was studied (gray lines, A-D) as well as VWF A2 glycan variants N1515Q, N1574Q (A), and N1515Q/N1574Q (B) and variants prepared in HEK293 GnT−/− deficient cells and following digestion with EndoH (C) and PNGase (D). Results are means ± standard error of the mean (SEM) of at least 3 independent experiments.

N-linked glycosylation stabilizes the VWF A2 domain through the N1574-GlcNAc linkage. DSF measurements, expressed as percent fluorescence (% FU), were carried out in the presence of 1 mM EDTA (open symbols) or 5 mM CaCl2 (closed symbols). WT VWF A2 was studied (gray lines, A-D) as well as VWF A2 glycan variants N1515Q, N1574Q (A), and N1515Q/N1574Q (B) and variants prepared in HEK293 GnT−/− deficient cells and following digestion with EndoH (C) and PNGase (D). Results are means ± standard error of the mean (SEM) of at least 3 independent experiments.

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