Abstract
Under standard assay conditions, the replicative DNA polymerase partially purified from rat liver non‐histone chromosomal proteins exhibited a marked preference for native DNA over heat‐denatured DNA as the template. However, work reported in the present paper demonstrates that this template preference could be reversed by changing the enzyme to template ratio in the assay system. This change in template preference was observed when either the concentration of DNA polymerase or of DNA was varied. Furthermore, it is shown that this alteration in template specificity is not the direct result of the action of an alkaline endonuclease present in the DNA polymerase preparation.
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