Infection of BHK 21 (C 13) or HEp-2 cells with herpes virus was followed by a marked increase in the activity of DNase which was prevented by actinomycin D and puromycin. Activation of a latent enzyme was not responsible for the increase. The properties of the DNase appearing after virus infection in both cell types were the same, but they differed from those of the enzyme from uninfected cells in specificity towards the secondary structure of the DNA substrate, heat-stability, requirement for thiol groups, inhibition by K and Na ions and response to various concentrations of Mg and Mn. The activities of DNase and phosphomonoesterase were not significantly altered after herpes infection. Further, the activity of RNase was not altered by infection, and this implies that the induced DNase was specific for DNA. The new DNase could be separated from the DNase present in uninfected cells and from phosphomonoesterase by chromatography on columns of DEAE-cellulose; its enzymic properties were the same as those observed with soluble extracts of cells infected with herpes virus.


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