J 2004

Cyclic voltammetric study of the redox system of glutathione using the disulfide bond reductant tris(2-carboxyethyl)phosphine

KIZEK, René, Jan VACEK, Libuše TRNKOVÁ and František JELEN

Basic information

Original name

Cyclic voltammetric study of the redox system of glutathione using the disulfide bond reductant tris(2-carboxyethyl)phosphine

Name in Czech

Cyklicko-voltametrická studie redox systému glutathione pomocí tris(2-carboxyethyl)phosphinu jako redukčního činidla disulfidických vazeb

Authors

KIZEK, René (203 Czech Republic), Jan VACEK (203 Czech Republic), Libuše TRNKOVÁ (203 Czech Republic, guarantor) and František JELEN (203 Czech Republic)

Edition

Bioelectrochemistry, The Netherlands, Elsevier, 2004, 1567-5394

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10405 Electrochemistry

Country of publisher

Netherlands

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 2.261

RIV identification code

RIV/00216224:14310/04:00011179

Organization unit

Faculty of Science

UT WoS

000221786900005

Keywords in English

voltammetry; hanging mercury drop electrode (HMDE); glutathione (GSH; GSSG); redox state; sulfhydryl and disulfide groups; tris(2-carboxyethyl)phosphine (TCEP); hydrogen peroxide

Tags

Změněno: 15/2/2005 21:49, prof. RNDr. Libuše Trnková, CSc.

Abstract

ORIG CZ

V originále

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 stateus 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/3M KCl did not disturb the signals of the thiol/disulfide redox couple. The origin of cathodic and anodic signals of GSH (at -0 .44 V and -0.37 V) and GSSG (at -0.69 V 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 behaviour.

In Czech

Cyklicko-voltametrická studie redox systému glutathione pomocí tris(2-carboxyethyl)phosphinu jako redukčního činidla disulfidických vazeb

Links

GA203/02/0422, research and development project
Name: Nové směry v elektrochemii nukleových kyselin a jejich aplikace v chemii životního prostředí
Investor: Czech Science Foundation, New trends in electrochemistry of nucleic acids and their applications in enviromental chemistry
IAA1163201, research and development project
Name: Využití adsorptivní přenosové a eliminační techniky pro elektrochemickou analýzu oligonukleotidů a nukleových kyselin
Investor: Academy of Sciences of the Czech Republic, Application of adsorptive transfer and elemination techniques in oligonucleotides and nucleic acids analysis.