Cyclic voltammetric study of the redox system of glutathione using the disulfide bond reductant tris(2-carboxyethyl)phosphine
Language English Country Netherlands Media print
Document type Evaluation Study, Journal Article, Research Support, Non-U.S. Gov't
PubMed
15110242
DOI
10.1016/j.bioelechem.2003.12.001
PII: S1567539404000052
Knihovny.cz E-resources
- MeSH
- Biocompatible Materials chemistry MeSH
- Disulfides analysis chemistry MeSH
- Electrochemistry methods MeSH
- Phosphines chemistry MeSH
- Glutathione analysis chemistry MeSH
- Glutathione Disulfide analysis chemistry MeSH
- Oxidation-Reduction MeSH
- Materials Testing methods MeSH
- Publication type
- Journal Article MeSH
- Evaluation Study MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Biocompatible Materials MeSH
- Disulfides MeSH
- Phosphines MeSH
- Glutathione MeSH
- Glutathione Disulfide MeSH
- tris(2-carboxyethyl)phosphine MeSH Browser
The stabilization of the reduction state of proteins and peptides is very important for the monitoring of protein-protein, protein-DNA and protein-xenobiotic interactions. The reductive state of protein or peptide is characterized by the reactive sulfhydryl group. Glutathione in the reduced (GSH) and oxidized (GSSG) forms was studied by cyclic voltammetry. Tris(2-carboxyethyl)phosphine (TCEP) as the disulfide bond reductant and/or hydrogen peroxide as the sulfhydryl group oxidant were used. Cyclic voltammetry measurements, following the redox state of glutathione, were performed on a hanging mercury drop electrode (HMDE) in borate buffer (pH 9.2). It was shown that in aqueous solutions TCEP was able to reduce disulfide groups smoothly and quantitatively. The TCEP response at -0.25 V vs. Ag/AgCl/3 M KCl did not disturb the signals of the thiol/disulfide redox couple. The origin of cathodic and anodic signals of GSH (at -0.44 and -0.37 V) and GSSG (at -0.69 and -0.40 V) glutathione forms is discussed. It was shown that the application of TCEP to the conservation of sulfhydryl groups in peptides and proteins can be useful instrument for the study of peptides and proteins redox behavior.
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