Purification and partial characterization of a DNA polymerase α species from calf thymus

Abstract
We have purified a DNA polymerase α species from calf thymus to near homogeneity. The enzyme sediments at 5.7 S and contains two polypeptides of 123000 and 134000 daltons in about equimolar ratio. The enzyme is inhibited by aphidicolin and N-ethylmaleimide, and retains its activity in buffers containing moderate salt conditions. Activated DNA is a better substrate than poly(dA)·(dt) 10.