The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Deoxyribonucleic acid polymerase from the extreme thermophile Thermus aquaticus
Open accessAbstract
A stable deoxyribonucleic acid (DNA) polymerase (EC 2.7.7.7) with a temperature optimum of 80 degrees C has been purified from the extreme thermophile Thermus aquaticus. The enzyme is free from phosphomonoesterase, phosphodiesterase and single-stranded exonuclease activities. Maximal activity of the enzyme requires all four deoxyribonucleotides and activated calf thymus DNA. An absolute requirement for divalent cation cofactor was satisfied by Mg2+ or to a lesser extent by Mn2+. Monovalent cations at concentrations as high as 0.1 M did not show a significant inhibitory effect. The pH optimum was 8.0 in tris(hydroxymethyl)aminomethane-hydrochloride buffer. The molecular weight of the enzyme was estimated by sucrose gradient centrifugation and gel filtrations on Sephadex G-100 to be approximately 63,000 to 68,000. The elevated temperature requirement, small size, and lack of nuclease activity distinguish this polymerase from the DNA polymerase of Escherichia coli.
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Cited by
Primer-Directed Enzymatic Amplification of DNA with a Thermostable DNA Polymerase
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How to increase value and reduce waste when research priorities are set
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Metadata
- Authors
- Chien, A., Edgar, D. B., & Trela, J. M.
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 1976-09
- Volume
- 127
- Issue
- 3
- Pages
- 1550-1557
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- OpenAlex
- W1629931862
- Cited by
- 699
- References
- 19
- FWCI
- 1.80
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Chien, A., Edgar, D. B., & Trela, J. M. (1976). Deoxyribonucleic acid polymerase from the extreme thermophile Thermus aquaticus. Journal of Bacteriology. https://doi.org/10.1128/jb.127.3.1550-1557.1976
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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