DNA Unwinding Enzyme II of Escherichia coli
- 1 September 1977
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 79 (1), 33-38
- https://doi.org/10.1111/j.1432-1033.1977.tb11780.x
Abstract
A DNA-stimulated ATP-.gamma.-phosphohydrolase of MW 75,000 was purified from E. coli cells. The ATPase [EC 3.6.1.3], a globular molecule (probably identical with an ATPase described previously) shows specificity for adenine nucleotides, it prefers single-stranded DNA as the cofactor, it exhibits a complicated mode of response to variations of the cofactor concentration and it is devoid of nuclease activity. Preparations derived from rep3 mutant cells yield widely varying amounts of an apparently normal ATPase.This publication has 18 references indexed in Scilit:
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