Figure 1.
Biological characterization of DGKKO. (A) Binding of KKO and DGKKO to microtiter wells coated with either hPF4 or hPF4 + UFH at different antibody concentrations. (B) The size of hPF4-UFH–antibody complexes determined using DLS over time in hours (hr). (C) Binding of 10 distinct HIT IgGs to microtiter wells coated with hPF4 + UFH in the presence of DGKKO (concentration, 0-5 μg/mL); n = 2; in duplicates. (D) Platelet activation via KKO vs DGKKO over a range of antibody concentrations assessed using surface P-selectin expression shown as geometric MFI. (E) Complement activation as indicated by C3c deposition on the platelet surface in the presence of KKO vs DGKKO. In panels A through E, the mean ± 1 SEM are shown. The number of independent experiments in each study is indicated in the figure. In panels C and D, P < .0001 using 2-way analysis of variance. MFI, mean fluorescent intensity; SEM, standard error of mean.

Biological characterization of DGKKO. (A) Binding of KKO and DGKKO to microtiter wells coated with either hPF4 or hPF4 + UFH at different antibody concentrations. (B) The size of hPF4-UFH–antibody complexes determined using DLS over time in hours (hr). (C) Binding of 10 distinct HIT IgGs to microtiter wells coated with hPF4 + UFH in the presence of DGKKO (concentration, 0-5 μg/mL); n = 2; in duplicates. (D) Platelet activation via KKO vs DGKKO over a range of antibody concentrations assessed using surface P-selectin expression shown as geometric MFI. (E) Complement activation as indicated by C3c deposition on the platelet surface in the presence of KKO vs DGKKO. In panels A through E, the mean ± 1 SEM are shown. The number of independent experiments in each study is indicated in the figure. In panels C and D, P < .0001 using 2-way analysis of variance. MFI, mean fluorescent intensity; SEM, standard error of mean.

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