Assessment of multimeric structure and ristocetin-induced binding to platelets of von Willebrand factor present in cryoprecipitate and different factor VIII concentrates.
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 AHF 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.
D001792:Blood Platelets / Q000187:drug effects / Q000378:metabolism; D011232:Chemical Precipitation; D005169:Factor VIII / Q000302:isolation & purification*; D005615:Freezing; D006801:Humans; D066298:In Vitro Techniques; D011487:Protein Conformation; D012310:Ristocetin / Q000494:pharmacology; D014841:von Willebrand Factor / Q000302:isolation & purification* / Q000378:metabolism
D014841:von Willebrand Factor; D012310:Ristocetin; D005169:Factor VIII