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Assessment of Multimeric Structure and Ristocetin‐Induced Binding to Platelets of Von Willebrand Factor Present in Cryoprecipitate and Different Factor VIII Concentrates
Author(s) -
LópezFernández M.F.,
LópezBerges C.,
Corral M.,
GarcíaTalavera J.R.,
Borrasca A. López,
Batlle J.
Publication year - 1987
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1987.tb02981.x
Subject(s) - cryoprecipitate , ristocetin , platelet , von willebrand factor , chemistry , antibody , microbiology and biotechnology , medicine , immunology , biology
. 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.