The DNA polymerase activity of vaccinia virus 'virosomes': solubilization and properties.

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 M-ammonium sulphate followed by brief sonication. The solubilized DNA polymerase activity from the 'virosomes', together with the DNA polymerases from 100000 g 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, Km for the deoxyribonucleoside triphosphates and the effect of N-ethylmaleimide.