THE RELATIONSHIP OF THE PROPERTIES OF ANTI-HEMOPHILIC FACTOR (FACTOR-VIII) THAT SUPPORT RISTOCETIN-INDUCED PLATELET AGGLUTINATION (FACTOR-VIIIR-RC) AND PLATELET RETENTION BY GLASS-BEADS AS DEMONSTRATED BY A MONOCLONAL-ANTIBODY

  • 1 January 1983
    • journal article
    • research article
    • Vol. 61  (1) , 27-35
Abstract
A monoclonal antibody to human antihemophilic factor (AHF, factor VIII) was derived from BALB/c mouse spleen cells fused with P3x63Ag8 mouse plasmacytoma cells. This antibody, harvested from culture medium or ascites fluid, reacted with purified AHF and with plasmas from normal subjects or classic hemophiliacs, as measured by enzyme-linked immunosorbant assay (ELISA), but not with plasmas from patients with severe von Willebrand''s disease. The antibody possessed only IgG1 H chains and .kappa. L chains. It blocked ristocetin-induced platelet agglutination and, to a lesser degree, platelet retention by glass bead columns, but it did not inhibit the procoagulant activity of AHF significantly. An amount of rabbit antiserum against AHF that provided equivalent inhibition of ristocetin-induced platelet agglutination inhibited glass bead retention much more effectively than did the mouse monoclonal antibody. This difference was exaggerated in studies of the corresponding Fab fragments. The site or sites on the AHF complex molecule that are associated with ristocetin-induced platelet agglutination differ quantitatively or qualitatively from those associated with enhancement of platelet retention by glass beads. ELISA titers of immunoreactive AHF, using the monoclonal antibody, were closely correlated to those using rabbit antiserum against AHF in normal, hemophilic and most von Willebrand''s disease plasmas.

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