Following SV 40 infection of monkey kidney (CV-1) cells, DNA polymerase activity was induced. Enzyme formation was inhibited by cycloheximide, but not by 1-β--arabinofuranosylcytosine. Enhanced levels of DNA polymerase activity were also found in mouse kidney cell lines which had been transformed by SV 40.

The DNA polymerases from uninfected and SV 40-infected CV-1 cells were partially purified and compared. Both enzymes required denatured DNA as primer and were similar with respect to pH optima, amount of primer required for maximal activity, kinetics of thermal denaturation, and sensitivity to inhibition by ammonium sulphate and sodium dodecyl sulphate. However, the Michaelis constant () for [H]thymidine 5′-triphosphate of the SV 40-induced enzyme was about half that of the enzyme from uninfected cells. The value of DNA polymerase partially purified from SV 40-transformed mouse cells was about the same as that of the enzyme from uninfected CV-1 cells.


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