Abstract
Preparations of E. coli dnaB gene product contain ribonucleoside triphosphatase activity that is stimulated 10-fold by DNA. The products of the triphosphatase activity are nucleoside diphosphates and P(i). The dnaB complementing activity in the varphiX174 DNA-dependent system and these triphosphatase activities copurify over the last 20-fold of an extensive (about 40,000-fold) purification procedure. Acrylamide gel electrophoresis of the purified material shows a single band of protein coincident with eluted dnaB complementing and DNA-dependent and -independent nucleoside triphosphatase activities.