Purification of Norman Murine Sarcoma DNA polymerase alpha forms with different DNA template primer binding affinity and different specific activity

Int J Biochem. 1989;21(2):203-8. doi: 10.1016/0020-711x(89)90110-9.


1. DNA polymerase alpha was isolated from Norman Murine Myxosarcoma cells using ion exchange, immunoaffinity, and DNA affinity chromatography, showing two distinct enzyme forms designated A1 and A2. 2. Chromatographic analysis of polymerase alpha forms A1 and A2 indicate a charge difference and a difference in affinity of binding to DNA between polymerase alpha forms which were equally reactive to anti-DNA polymerase alpha monoclonal IgG. 3. Polymerase A1 specific activity was about 3600 U/mg while A2 specific activity was about 40,000 U/mg.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Binding Sites
  • Chromatography, Affinity
  • Chromatography, DEAE-Cellulose
  • Chromatography, High Pressure Liquid
  • Chromatography, Ion Exchange
  • DNA Polymerase II / isolation & purification*
  • Isoenzymes / isolation & purification*
  • Mice
  • Molecular Weight
  • Myxosarcoma / enzymology*
  • Sarcoma / enzymology*
  • Substrate Specificity


  • Isoenzymes
  • DNA Polymerase II