Peptide mapping of the four subunits of the mouse DNA polymerase alpha-primase complex

Biochem Biophys Res Commun. 1990 Jul 31;170(2):589-95. doi: 10.1016/0006-291x(90)92132-j.


We report a simple, two-step method (phosphocellulose and immunoaffinity column chromatographies) for purification of the mouse DNA polymerase alpha-primase complex. The advantages of this method over other procedures are its simplicity and rapidity, with little loss by proteolysis. Sedimentation analysis in a glycerol density gradient of the immunoaffinity-purified fraction revealed that four polypeptides with molecular weights of 180,000, 68,000, 54,000 and 46,000 in the enzyme fraction form a physical complex. Peptide mapping by reversed phase-high performance liquid chromatography demonstrated unequivocally that these four polypeptides constituting the complex are different entities.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cells, Cultured
  • Chromatography, Affinity
  • Chromatography, High Pressure Liquid
  • DNA Primase
  • Mice
  • Mice, Inbred BALB C
  • Mice, Inbred C3H
  • Peptide Mapping
  • RNA Nucleotidyltransferases / isolation & purification*


  • DNA Primase
  • RNA Nucleotidyltransferases