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Structure‐Function of the Factor VIII Complex Studied with an Immobilized Heteroantisera to VIII:C
Author(s) -
Cooper Herbert A.,
Lee Dorothy,
Lamb Mary Ann,
Wagner Robert H.
Publication year - 1980
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1980.tb01192.x
Subject(s) - chemistry , antibody , agarose , immune system , von willebrand factor , chromatography , platelet , immune complex , antigen , ristocetin , coagulation , antigen antibody complex , factor vii , microbiology and biotechnology , immunology , medicine , biology
S ummary . An antibody was raised in rabbits to the small active fragment of human factor VIII, obtained by Ca 2+ dissociation of a human factor VIII preparation made from a multidonor plasma pool. After absorption, the antibody neutralized the factor VIII coagulant activity of normal human plasma, but did not precipitate with any plasma or plasma fractions or neutralize von Willebrand factor (vWF) activity as measured by ristocetin aggregation of fixed washed platelets. Immune beads were prepared by CNBr binding of the partially purified rabbit antibody to 1% agarose beads. Non‐immune beads were prepared with IgG fractions obtained from the rabbits before immunization and used throughout as a control. The amount of factor VIII coagulant activity (VIII:C) removed from plasma by immune beads was time‐dependent and proportional to the amount of beads used, but all of the VIII:C could not be readily removed. Removal of VIII:C by immune beads parallelled removal of factor VIII:antigen, but less vWF activity was removed. Immune beads could be blocked or saturated by treatment with large amounts of normal plasma, but not by von Willebrand disease plasma and only by some haemophilic plasmas.