Intracellular DNA-protein complexes (‘virosomes’) of vaccinia virus have been isolated. The solubilization of the ‘virosome’-bound DNA polymerase activity was attempted by a variety of high-salt extraction procedures. The most efficient of these used 0.3 -ammonium sulphate followed by brief sonication. The solubilized DNA polymerase activity from the ‘virosomes’, together with the DNA polymerases from 100000 supernatant fluids from the cytoplasm of infected and uninfected cells were chromatographed on DEAE-cellulose and their properties compared. The ‘virosome’ DNA polymerase activity differed from the soluble vaccinia virus-induced DNA polymerase activity in its requirements for divalent cations and in respect of pH optimum, for the deoxyribonucleoside triphosphates and the effect of -ethylmaleimide.


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