The multimeric structure of von Willebrand factor (vWF) and its ristocetin-induced binding to platelets,
using a simple and very sensitive radiomonoclonal antibody-labeled vWF method, was compared in normal plasma,
single-donor cryoprecipitate (CP) and five different antihemophilic factor (AHF) concentrates. All the AFIF showed a
lack of larger vWF multimers, an abnormal ‘triplet’ pattern, and much lower vWF binding to platelets than that of
plasma or CP, vWF being the lowest for those with a lesser proportion of larger vWF multimers. These results suggest
that the combination of vWF multimeric analysis and the radiomonoclonal-labeled vWF method may be very useful
in the assessment of AHF preparations.
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