Sensitive electrochemical determination of unlabeled MutS protein and detection of point mutations in DNA
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
15456317
DOI
10.1021/ac049474x
Knihovny.cz E-resources
- MeSH
- Point Mutation genetics MeSH
- DNA, Bacterial analysis chemistry genetics metabolism MeSH
- Electrochemistry methods MeSH
- Electrodes MeSH
- Catalysis MeSH
- Oxidation-Reduction MeSH
- Mercury chemistry MeSH
- Sensitivity and Specificity MeSH
- Thermus chemistry genetics MeSH
- Tyrosine chemistry metabolism MeSH
- Carbon chemistry MeSH
- Protein Binding MeSH
- MutS DNA Mismatch-Binding Protein analysis chemistry metabolism MeSH
- Hydrogen chemistry metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- DNA, Bacterial MeSH
- Mercury MeSH
- Tyrosine MeSH
- Carbon MeSH
- MutS DNA Mismatch-Binding Protein MeSH
- Hydrogen MeSH
MutS protein plays an important role in the DNA repair system in prokaryotic and eukaryotic cells; it recognizes unpaired and mispaired bases in duplex DNA and can be used for detection of point mutations in vitro. We have shown that small amounts of this protein can be detected electrochemically at mercury and carbon electrodes without any labeling. Using constant current stripping analysis (CPSA) and mercury electrodes, tens of attomoles of this protein can be detected. The sensitivity of the determination at carbon electrodes is by more than 3 orders of magnitude lower. Using biotinylated DNA duplexes attached to magnetic beads, single-base mismatches and insertion/deletions were recognized by MutS. Picogram amounts of this protein were detected by CPSA after MutS releasing from the beads.
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