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A Deoxyribonucleic Acid Phosphatase-Exonuclease from Escherichia coli
Open accessAbstract
An enzyme detected initially by its capacity to increase the priming capacity of deoxyribonucleic acid was ident.ified upon its purification from Escheriehia coli extracts as a phosphatase acting specifically on 3’-phosphoryl-terminated deoxyribonucleic acid chains (1, 2). Concurrent with the purification of this DNA phosphatase, there was an enrichment for an exonucleolytic activity which could be distinguished from the two known exonucleases of E. coli. Evidence for the identity of the phosphatase and exonuclease activities with a single enzyme is the subject of this report and the basis for naming this enzyme a DNA phosphatase-exonuclease. The specificity of the enzyme in attacking native double stranded DNA and its inability to act on small polynucleotides make it a unique and useful reagent in studies of DN-4 structure and metabolism.
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Cited by
Enzymatic Synthesis of Deoxyribonucleic Acid
Richardson, C. C., Schildkraut, C. L., Aposhian, H. V., & Kornberg, A. (1964) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)51772-5 · Cited by 718
Self-citationPhosphorylation of nucleic acid by an enzyme from T4 bacteriophage-infected Escherichia coli.
Richardson, C. C. (1965) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.54.1.158 · Cited by 607
Self-citationNew RNA Polymerase from Escherichia coli infected with Bacteriophage T7
CHAMBERLIN, M., MCGRATH, J., & WASKELL, L. (1970) · Nature · doi:10.1038/228227a0 · Cited by 543
The Chemistry of Self-Splicing RNA and RNA Enzymes
Cech, T. R. (1987) · Science · doi:10.1126/science.2438771 · Cited by 531
The Deoxyribonucleases of Escherichia coli
Lehman, I. R., & Nussbaum, A. L. (1964) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93898-6 · Cited by 393
Metadata
- Authors
- Richardson, C. C., & Kornberg, A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1964-01
- Volume
- 239
- Issue
- 1
- Pages
- 242-250
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W88565723
- Cited by
- 336
- References
- 0
- FWCI
- 25.61
- Type
- journal article
- Language
- en
- Open access
- hybrid
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