Monoclonal antibody specific for chicken DNA polymerase alpha associated with DNA primase

Biochem Biophys Res Commun. 1985 Oct 15;132(1):210-6. doi: 10.1016/0006-291x(85)91009-5.


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

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal*
  • Antibody Specificity
  • Binding, Competitive
  • Chick Embryo
  • Chromatography, Affinity
  • DNA Polymerase II / immunology*
  • DNA Polymerase II / metabolism
  • DNA Primase
  • Enzyme-Linked Immunosorbent Assay
  • Epitopes / analysis
  • Methods
  • Mice
  • RNA Nucleotidyltransferases / metabolism*


  • Antibodies, Monoclonal
  • Epitopes
  • DNA Primase
  • RNA Nucleotidyltransferases
  • DNA Polymerase II