Determination of glutathione-S-transferase traces in preparations of p53 C-terminal domain (aa320-393)
Language English Country Netherlands Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
11786354
DOI
10.1016/s1567-5394(01)00137-2
PII: S1567539401001372
Knihovny.cz E-resources
- MeSH
- Glutathione Transferase analysis MeSH
- Tumor Suppressor Protein p53 chemistry MeSH
- Potentiometry MeSH
- Recombinant Fusion Proteins chemistry MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Glutathione Transferase MeSH
- Tumor Suppressor Protein p53 MeSH
- Recombinant Fusion Proteins MeSH
Tumor suppressor protein p53 is often expressed as a fusion protein with glutathione-S-transferase (GST). The sensitive determination of GST in p53 samples is thus necessary. We propose a method for the determination of traces of GST in the p53 C-terminus based on the constant current chronopotentiometric stripping analysis (CPSA) with hanging mercury drop electrode (HMDE). GST produces a catalytic signal in cobalt-containing solutions due to cysteine residues. A large excess of the C-terminus does interfere with the determination because of the lack of cysteines in the molecule. This method is simple and very sensitive and is capable of detecting <1% GST in the p53 sample.
References provided by Crossref.org
Preferential binding of hot spot mutant p53 proteins to supercoiled DNA in vitro and in cells
Role of tumor suppressor p53 domains in selective binding to supercoiled DNA