Figure 3
Figure 3. Binding of VWF mutants to different Mabs. Various concentrations (0-1 μg/mL) of wt-rVWF (▪), p.L1696R-rVWF (○), or p.P1824H-VWF (△) were incubated with microtiter wells coated with 1 of the indicated Mabs (418, 318, 701, 724, 487, 9, 200, or 505). Bound VWF was probed using horseradish peroxidase–labeled polyclonal anti-VWF antibodies and detected via peroxidase hydrolysis of Tetramethylbenzidine. Presented is the relative response (% of binding by wt-rVWF at 1 μg/mL) vs VWF:Ag concentration (μg/mL). The drawn lines represent the best fit using an equation for one-site–specific binding using GraphPad Prism software. Data represent the mean ± SD of 3 independent measurements.

Binding of VWF mutants to different Mabs. Various concentrations (0-1 μg/mL) of wt-rVWF (▪), p.L1696R-rVWF (○), or p.P1824H-VWF (△) were incubated with microtiter wells coated with 1 of the indicated Mabs (418, 318, 701, 724, 487, 9, 200, or 505). Bound VWF was probed using horseradish peroxidase–labeled polyclonal anti-VWF antibodies and detected via peroxidase hydrolysis of Tetramethylbenzidine. Presented is the relative response (% of binding by wt-rVWF at 1 μg/mL) vs VWF:Ag concentration (μg/mL). The drawn lines represent the best fit using an equation for one-site–specific binding using GraphPad Prism software. Data represent the mean ± SD of 3 independent measurements.

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