Five monoclonal antibodies to human von Willebrand factor were selected for characterization
from 18 produced in murine hybridomas. All showed a high and specific affinity for
human von Willebrand factor (vWf) but exhibited little if any crossreaction with sera
from other species. The antibodies defined four epitopes on vWf, none of which were
involved in platelet binding. Binding of two distinct antibodies at one of these epitopes
was associated with enhancement of the rate of vWf-dependent platelet agglutination
in the presence of ristocetin. This effect was more noticeable when cryosupernatant
plasma was used in place of normal plasma as the source of vWf, and was not explicable
simply in terms of antibody-induced cross-linking of vWf.
Keywords
Factor VIII - von Willebrand factor - Ristocetin cofactor - Monoclonal antibody