Figure 2.
Kinetic inhibition of plasma ADAMTS13 by various antispacer antibodies (scFv20, scFv3-1, and scFv4-16). (A) Cartoon representation of the structure of ADAMTS13, as described in Figure 1. Spacer domain, the binding site of scFv4-20, scFv3-1, and scFv4-16 to ADAMTS13, is indicated by an arrow. Assays were performed at 25°C and pH 6.0. (B) Relative inhibitory activity variation of scFv4-20 incubated with NHP for different lengths of time (0, 30, 60, 90, 120, and 180 minutes). Activity was normalized to velocity (ΔFU/s) in the absence of scFv4-20 (buffer control) to derive relative velocity. (C-E) The titrations of ADAMTS13 in NHP with FRETS-VWF73 in the presence of increasing concentrations of scFv4-20, scFv3-1, and scFv4-16, respectively (n ≥ 3 for all titrations). The data in the plots are shown as mean ± SEM.

Kinetic inhibition of plasma ADAMTS13 by various antispacer antibodies (scFv20, scFv3-1, and scFv4-16). (A) Cartoon representation of the structure of ADAMTS13, as described in Figure 1. Spacer domain, the binding site of scFv4-20, scFv3-1, and scFv4-16 to ADAMTS13, is indicated by an arrow. Assays were performed at 25°C and pH 6.0. (B) Relative inhibitory activity variation of scFv4-20 incubated with NHP for different lengths of time (0, 30, 60, 90, 120, and 180 minutes). Activity was normalized to velocity (ΔFU/s) in the absence of scFv4-20 (buffer control) to derive relative velocity. (C-E) The titrations of ADAMTS13 in NHP with FRETS-VWF73 in the presence of increasing concentrations of scFv4-20, scFv3-1, and scFv4-16, respectively (n ≥ 3 for all titrations). The data in the plots are shown as mean ± SEM.

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