Binding of ADAMTS13 to von Willebrand factor.

摘要: Abstract ADAMTS13, a metalloprotease, cleaves von Willebrand factor (VWF) in plasma to generate smaller, less thrombogenic fragments. The interaction of with specific ADAMTS13 domains was characterized binding assay employing immobilized on plastic surface. saturable and reversible. Equilibrium occurred within 2 h the half-time for dissociation ∼4 h. Binding similar either recombinant or normal ADAMTS13; from patient who lacked activity showed no binding. stoichiometry one per two monomers, Kd 14 nm. metalloprotease disintegrin did not bind VWF detectably. truncated after first thrombospondin type 1 repeat bound 206 nm, whereas spacer domain had 23 which is comparable that full-length ADAMTS13. Truncation eighth reduced affinity by ∼3-fold truncation seventh addition CUB increased ∼2-fold. Therefore, required factor. also affects binding, C-terminal may modulate this interaction.