PURIFIED COMPLEX OF FACTOR-VIII COAGULANT MOIETY AND PHOSPHOLIPID - HIGH FACTOR-VIII COAGULANT ACTIVITY IN FACTOR-VIII INHIBITOR PLASMA

  • 1 January 1984
    • journal article
    • research article
    • Vol. 96  (22) , 829-832
Abstract
A complex of factor VIII coagulant moiety and phospholipid was purified by means of immunoadsorbent chromatography of factor VIII concentrate and consecutive dissociation of the immobilized factor VIII complex by human placental phospholipid (Fibraccel). The complex of factor VIII coagulant moiety and phospholipid displayed factor VIII coagulant activity (VIIIC) and factor VIII coagulant antigen (VIIIC:Ag), but no factor VIII related antigen (VIIIR:Ag). When incubated with factor VIII inhibitor plasma, the complex of factor VIII coagulant moiety and phospholipid exerted higher factor VIII coagulant activity than native factor VIII complex, and than purified factor VIII coagulant moiety alone. Results prove that in activated prothrombin complex concentrates a complex of factor VIII coagulant moiety and phospholipid is the active mechanism, exerting procoagulant activity in factor VIII inhibitor plasma. [This research has implications for hemophilia studies.].

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