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Monoclonal anti-LDL antibodies were produced in a mouse spleen-myeloma system and purified by affinity chromatography on insolubilized low density lipoprotein (LDL). Five antibodies with different specificities could be distinguished by their immunoreactivities with chemically modified LDL preparations, and by their competition for binding to LDL. One of the antibodies inhibited the binding of (125)I-labeled LDL to the apoB,E receptors of cultured human fibroblasts. The same degree of inhibition was achieved using isolated Fab fragments. This antibody may bind to an antigenic site located near the cellular binding site of LDL-apoB.-Tikkanen, M. J., R. Dargar, B. Pfleger, B. Gonen, J. M. Davie, and G. Schonfeld. Antigenic mapping of human low density lipoprotein with monoclonal antibodies.
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