Inhibition of the binding of 125I-bitiscetin to immobilized vWF by MoAb directed against vWF. Purified vWF (10 μg/mL) was coated onto wells of microtiter plates.125I-bitiscetin (2 × 105 cpm, 100 μL/well) premixed with various concentrations of competitor was then incubated. After washing, the bound radioactivity was counted. Nonspecific binding was estimated using buffer instead of vWF for coating. Results are expressed as the percent of the specific binding measured in the absence of competitor (100%). This value of specific binding represents a bound radioactivity of ≠15% of the total. (A) MoAb directed against the A3 domain of vWF: MoAb 201 (◊); 400 (▴); 505 (○); 535 (□). MoAb 454 (•) was used as control. (B) MoAb directed against the A1 domain of vWF: MoAb 701(▴); 710 (◊); 724 (○); 322 (▪).
