Abstract
Four monoclonal antibodies against chicken DNA polymerase α were obtained from mouse hybridomas (see ref. 1). Two of them, 4-2D and 4–8H, recognized different epitopes of the DNA polymerase α-DNA primase complex as determined by a competitive enzyme-linked immunosorbent assay. Antibody 4–8H partially (about 30%) neutralized the combined activity of primase-DNA polymerase α as well as the DNA polymerase α activity. In contrast, antibody 4-2D did not neutralize DNA polymerase α activity, but neutralized the primase-DNA polymerase α activity extensively (up to 80%). Furthermore, although an immunoaffinity column made with 4–8H antibody retained virtually all of the DNA polymerase α with and without associated primase, a column made with 4-2D antibody did not bind DNA polymerase α without the primase, but retained the enzyme associated with the primase. These results indicate that 4–8H monoclonal antibody is specific for DNA polymerase α and 4-2D monoclonal antibody is specific for the primase or a special structure present in the primase-DNA polymerase α complex.
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