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We have established a solid phase binding assay using biotinylated fibrinogen as a ligand. Biotinylation did not alter its binding capacity and affinity to solid phase GPIIb/IIIa. Biotinylated fibrinogen binding, as measured by color development of enzymatic reaction, was specific, time-dependent, reversible, saturable and divalent cation-dependent. Unlabeled fibrinogen and three peptide fragments of fibrinogen, RGDV, RGDS and HHLGGAKQAGDV (gamma-chain 400-411) competitively inhibited the binding with IC50 values of 3.7, 49, 155 and 715nM, respectively. The apparent dissociation constant (Kd) of biotinylated fibrinogen was determined to be 0.33nM.This simple and high-flux solid phase binding assay can be useful to directly detect the binding between fibrinogen and GPIIb/IIIa.

Establishment of Solid Phase GPIIb/IIIa Binding Assay Using Biotinylated Fibrinogen as a Ligand