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:
- Enzymatic unwinding of DNAJournal of Molecular Biology, 1977
- A mechanism of duplex DNA replication revealed by enzymatic studies of phage phi X174: catalytic strand separation in advance of replication.Proceedings of the National Academy of Sciences, 1977
- Enzymic Unwinding of DNAEuropean Journal of Biochemistry, 1976
- Enzymic Unwinding of DNAEuropean Journal of Biochemistry, 1976
- An ATPase Depending an the Presence of Single‐Stranded DNA from Mouse MyelomaEuropean Journal of Biochemistry, 1976
- The rep mutationJournal of Molecular Biology, 1975
- The rep mutationVirology, 1972
- Affinity Chromatography of DNA‐Binding Enzymes on Single‐Stranded DNA‐Agarose ColumnsEuropean Journal of Biochemistry, 1972
- Some aspects of the use of “continuous” and “discontinuous” buffer systems in polyacrylamide gel electrophoresisAnalytical Biochemistry, 1965
- Colorimetric Determination of Inorganic Phosphate in Microgram QuantitiesAnalytical Chemistry, 1951