Abstract
A modified purification is described for an enzyme, from Escherichia coli B, which polymerizes deoxyribonucleoside-5′ diphosphates. Under appropriate conditions, the enzyme will add a single deoxyribonucleotide residue to a deoxyribo-oligonucleotide primer. At all stages, the enzyme activity copurified with the activity which will polymerize adenosine-5′ diphosphate (polynucleotide phosphorylase). Studies of heat stability, the effect of various temperatures of reaction and of disc gel electrophoresis failed to provide evidence that the two activities are separable.
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