Assessment of Multimeric Structure and Ristocetin-Induced Binding to Platelets of Von Willebrand Factor Present in Cryoprecipitate and Different Factor VIII Concentrates |
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Authors: | M.F. Ló pez-Ferná ndez MD,,C. Ló pez-Berges,M. Corral,J.R. Garcí a-Talavera,A. Ló pez Borrasca,and J. Batlle |
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Affiliation: | Division of Hematology-Hemotherapy, Hospital Clínico, University of Salamanca, Spain;Department of Nuclear Medicine, Hospital Clínico, University of Salamanca, Spain |
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Abstract: | 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. |
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