Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Improved PCR performance using mutant Tpa-S DNA polymerases from the hyperthermophilic archaeon Thermococcus pacificus.

Journal of biotechnology - 15 Dec 2012

Ppyun Hyewoo, Kim Inhye, Cho Sung Suk, Seo Kang Jin, Yoon Keejung, Kwon Suk-Tae

Abstract excerpt

We previously reported that Tpa-S DNA polymerase (constructed via fusion of the Sso7d DNA binding protein to the C-terminus of Thermococcus pacificus (Tpa) DNA polymerase) is more efficient in long and rapid PCR than wild-type Tpa, Taq, or Pfu DNA polymerases. However, Tpa-S DNA polymerase had a low yield of PCR products compared with commercialized Taq or Pfu DNA polymerases. To improve the yield of PCR...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cloning, Molecular
Share to DNA-Directed DNA Polymerase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Hydrogen-Ion Concentration

Share to Kinetics

Share to Plasmids

Share to Potassium Chloride

Share to Recombinant Proteins

Source

Identifiers

PMID: 23395617
DOI: 10.1016/j.jbiotec.2013.01.022

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Improved PCR performance using mutant Tpa-S DNA polymerases from the hyperthermophilic archaeon Thermococcus pacificus.PMID 23395617Read ↗

Engineering of DNA polymerase I from Thermus thermophilus using compartmentalized self-replication.Semantic proximity Read ↗

Improvements of rolling circle amplification (RCA) efficiency and accuracy using Thermus thermophilus SSB mutant protein.Semantic proximity Read ↗

Increased Processivity, Misincorporation, and Nucleotide Incorporation Efficiency in Sulfolobus solfataricus Dpo4 Thumb Domain Mutants.Semantic proximity Read ↗

Circular permutation engineering improves amplification efficiency of Bst DNA polymerase.Semantic proximity Read ↗

Design and Discovery of New Combinations of Mutant DNA Polymerases and Modified DNA Substrates.Semantic proximity Read ↗

Mutations to create thermostable reverse transcriptase with bacterial family A DNA polymerase from Thermotoga petrophila K4.Semantic proximity Read ↗

Enhancement of Polymerase Activity of the Large Fragment in DNA Polymerase I from Geobacillus stearothermophilus by Site-Directed Mutagenesis at the Active Site.Semantic proximity Read ↗

Enhancing the processivity of a family B-type DNA polymerase of Thermococcus onnurineus and application to long PCR.Semantic proximity Read ↗

Engineering of T7 DNA-dependent RNA polymerase with activity at elevated temperature.Semantic proximity Read ↗

Mutations in the palm subdomain of Twa DNA polymerase to enhance PCR efficiency and its function analysis.Semantic proximity Read ↗

A simple and general approach to control the activity of DNA processing enzymesSemantic proximity Read ↗

Efficiency and Fidelity of Site-Directed Mutagenesis with Complementary Primer Pairs.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.