Abstract
A mutant PAD-1(D514→Q) of the recombinant fragment PAD-1 comprising Leu469-Ser723 Of the A1 domain of bovine von Willebrand factor (vWF) neither inhibited the binding of [125I]vWF to platelets nor the agglutination of human platelets induced by bovine VWF. PAD-1, on the other hand, inhibited human platelet agglutination induced by bovine VWF and [125I]vWF binding to human platelets. Collagen binding properties of the mutant, however, were indistinguishable from those of PAD-1. These results suggested that Asp514 within the A1 domain of vWF is required for interaction of bovine vWF with GPIb receptor on human platelets.
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