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Abstract
Two forms of DNA polymerase alpha were separated from HeLa cells by DEAE-cellulose column chromatography and affinity chromatography using a DNA-cellulose column. They were eluted from a DEAE-cellulose column at 0.22M KCl (P-I) and 0.24M KCl (P-II). Upon cell fractionation between cytosol and nuclei, P-I was recovered from nuclei and P-II from cytosol. P-I was found to have a higher binding affinity to DNA than P-II by DNA-cellulose column chromatography.
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