Figure 4.
Direct binding of the FV mutants to EGR-APC and PS by a fluid-phase SPR-based assay. (A) EGR-APC binding. Various concentrations of FV mutants (WT, A2086D, W1920R, and R506Q) were added to EGR-APC (700 RU) immobilized on the sensor chip for 4 minutes, followed by a change of running buffer for 4 minutes. The lines show representative curves for FV mutants at 7.8, 15.6, 31.3, and 62.5 nM, and the fitted curves prepared using a 1-site binding model are shown (solid thin line). (B) PS binding. Various concentrations of FV mutants (WT, A2086D, W1920R, and R506Q) were added to PS (3000 RU) immobilized on the sensor chip for 2 minutes, followed by a change of running buffer for 2 minutes. The lines show representative curves for FV mutants at 3.9, 7.8, 15.6, and 31.3 nM, and fitted curves prepared using a 1-site binding model are shown (solid thin line).

Direct binding of the FV mutants to EGR-APC and PS by a fluid-phase SPR-based assay. (A) EGR-APC binding. Various concentrations of FV mutants (WT, A2086D, W1920R, and R506Q) were added to EGR-APC (700 RU) immobilized on the sensor chip for 4 minutes, followed by a change of running buffer for 4 minutes. The lines show representative curves for FV mutants at 7.8, 15.6, 31.3, and 62.5 nM, and the fitted curves prepared using a 1-site binding model are shown (solid thin line). (B) PS binding. Various concentrations of FV mutants (WT, A2086D, W1920R, and R506Q) were added to PS (3000 RU) immobilized on the sensor chip for 2 minutes, followed by a change of running buffer for 2 minutes. The lines show representative curves for FV mutants at 3.9, 7.8, 15.6, and 31.3 nM, and fitted curves prepared using a 1-site binding model are shown (solid thin line).

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