Please use this identifier to cite or link to this item:
https://hdl.handle.net/10316/27835
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Enache, Teodor Adrian | - |
dc.contributor.author | Brett, Ana Maria Oliveira | - |
dc.date.accessioned | 2014-12-09T16:07:20Z | - |
dc.date.available | 2014-12-09T16:07:20Z | - |
dc.date.issued | 2015-02 | - |
dc.identifier.citation | ENACHE, Teodor Adrian; OLIVEIRA-BRETT, Ana Maria - Electrochemical evaluation of glutathione S-transferase kinetic parameters. "Bioelectrochemistry". ISSN 1567-5394. Vol. 101 (2014) p. 46–51 | por |
dc.identifier.issn | 1567-5394 | - |
dc.identifier.uri | https://hdl.handle.net/10316/27835 | - |
dc.description.abstract | Glutathione S-transferases (GSTs), are a family of enzymes belonging to the phase II metabolism that catalyse the formation of thioether conjugates between the endogenous tripeptide glutathione and xenobiotic compounds. The voltammetric behaviour of glutathione (GSH), 1-chloro-2,4-dinitrobenzene (CDNB) and glutathione S-transferase (GST), as well as the catalytic conjugation reaction of GSH to CDNB by GST was investigated at room temperature, T = 298.15 K (25 °C), at pH 6.5, for low concentration of substrates and enzyme, using differential pulse (DP) voltammetry at a glassy carbon electrode. Only GSH can be oxidized; a sensitivity of 0.14 nA/μM and a LOD of 6.4 μM were obtained. The GST kinetic parameter electrochemical evaluation, in relation to its substrates, GSH and CDNB, using reciprocal Michaelis–Menten and Lineweaver–Burk double reciprocal plots, was determined. A value of KM ~ 100 μM was obtained for either GSH or CDNB, and Vmax varied between 40 and 60 μmol/min per mg of GST. | por |
dc.language.iso | eng | por |
dc.publisher | Elsevier | por |
dc.rights | openAccess | por |
dc.subject | Glutathione | por |
dc.subject | 1-Chloro-2,4-dinitrobenzene | por |
dc.subject | Glutathione S-transferase | por |
dc.subject | Electrochemistry | por |
dc.subject | Oxidation | por |
dc.title | Electrochemical evaluation of glutathione S-transferase kinetic parameters | por |
dc.type | article | por |
degois.publication.firstPage | 46 | por |
degois.publication.lastPage | 51 | por |
degois.publication.title | Bioelectrochemistry | por |
dc.relation.publisherversion | http://www.sciencedirect.com/science/article/pii/S156753941400108X | por |
dc.peerreviewed | Yes | por |
dc.identifier.doi | 10.1016/j.bioelechem.2014.07.002 | - |
degois.publication.volume | 101 | por |
item.openairetype | article | - |
item.languageiso639-1 | en | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.cerifentitytype | Publications | - |
item.grantfulltext | open | - |
item.fulltext | Com Texto completo | - |
crisitem.author.researchunit | CEMMPRE - Centre for Mechanical Engineering, Materials and Processes | - |
crisitem.author.researchunit | CEMMPRE - Centre for Mechanical Engineering, Materials and Processes | - |
crisitem.author.orcid | 0000-0002-1848-6753 | - |
crisitem.author.orcid | 0000-0002-6244-0891 | - |
Appears in Collections: | FCTUC Química - Artigos em Revistas Internacionais |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Electrochemical evaluation of glutathione.pdf | 1.09 MB | Adobe PDF | View/Open |
SCOPUSTM
Citations
20
checked on Mar 18, 2024
WEB OF SCIENCETM
Citations
5
18
checked on Mar 2, 2024
Page view(s)
306
checked on Mar 26, 2024
Download(s) 50
660
checked on Mar 26, 2024
Google ScholarTM
Check
Altmetric
Altmetric
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.