Immunogenicity of the chimeric plasminogen activator K2tu-PA in rabbits.
Rabbits were repeatedly immunized with a chimeric plasminogen activator composed of the kringle-2 domain of human tissue-type plasminogen activator (t-PA) attached to the serine protease domain of the human urokinase-type plasminogen activator (u-PA). IgG from these rabbits was purified, biotinylated and subjected to affinity chromatography on K2tu-PA covalently attached to Sepharose. Roughly half the antibodies recovered from the K2tu-PA column could subsequently be bound to a column with similarly immobilized t-PA, whereas the other half bound to a u-PA column. Less than 0.01% of the biotinylated anti-K2tu-PA antibodies did not bind to either t-PA or u-PA and perhaps are directed against neoantigenic determinants on K2tu-PA, not present in the natural plasminogen activators.
Asselbergs
F A
FA
Biotechnology Department, Ciba-Geigy Ltd, Basle, Switzerland.
D000818:Animals; D000941:Antigens / Q000276:immunology*; D001710:Biotin; D002846:Chromatography, Affinity; D007074:Immunoglobulin G / Q000302:isolation & purification; D018082:Kringles; D011817:Rabbits; D011993:Recombinant Fusion Proteins / Q000276:immunology*; D010959:Tissue Plasminogen Activator / Q000276:immunology*; D014568:Urokinase-Type Plasminogen Activator / Q000276:immunology*
D000941:Antigens; D007074:Immunoglobulin G; D011993:Recombinant Fusion Proteins; D001710:Biotin; D010959:Tissue Plasminogen Activator; D014568:Urokinase-Type Plasminogen Activator