Purification and Properties of a DNA-Dependent ATPase Induced by Bacteriophage T4

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Abstract
A DNA-dependent ATPase [EC 3.6.1.-] formed after T4 phage infection [of Escherichia coli] is purified to apparent homogenity. The MW of the purified enzyme is 50,000 when determined by glycerol gradient centrifugation and by sodium dodecylsulfate/polyacrylamide gel electrophoresis. The enzyme at an earlier stage in purification (prior to DEAE-cellulose chromatography) exists as a complex with a MW of 100,000. MW determinations by Sephadex gel chromatography give considerably decreased MW for the complex and for the enzyme after DEAE-cellulose chromatography. The enzyme is stimulated to varying degrees by several single-stranded polydeoxyribonucleotides or by single-stranded DNA, but no chemical change in the polynucleotide was detected as a result of the enzyme action.