Abstract
Monoclonal antibodies (MoAbs) to human alpha-fetoprotein (AFP) produced by 13 different murine hybridoma clones were used in affinity electrophoresis. The binding of MoAbs to AFP was studied in different experimental systems: crossed affinity immunoelectrophoresis, rocket affinity immunoelectrophoresis and zone affinity electrophoresis in agarose. Experimental data indicated that MoAb-AFP and AFP-MoAb-AFP complexes were formed during electrophoresis. Affinity electrophoresis seems to be a convenient and sensitive method for studies on the reaction of monoclonal antibodies with their antigens. In addition, the technique offers the possibility of calculating the dissociation constants of MoAb-AFP and of AFP-MoAb-AFP complexes and evaluating the reaction of MoAbs with different antigenic determinants.
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