Abstract
An endonucleolytic activity is associated with purified PM2 bacteriophages. It converts the double-stranded supercoiled PM2 DNA mostly into the linear form that sediments as a homogenous peak in alkaline sucrose gradients. The same activity is found in intact or detergent-lysed phages. Optimal activity is observed between pH 6.8 and 7.5 at 28°. Divalent cations, Mg2+ or Mn2+, are necessary for activity, and the enzyme is inhibited by RNA. The endonuclease has no appreciable activity on linear DNA molecules, but it attacks single-stranded circular DNA.
Keywords: DNase; zone sedimentation; electron microscopy; PM2, simian virus 40, and fd supercoiled DNA
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Selected References
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