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dc.contributor.authorMartos Maldonado, Manuel Cristo 
dc.contributor.authorCasas Solvas, Juan Manuel 
dc.contributor.authorVargas Berenguel, Antonio 
dc.contributor.authorGarcía Fuentes, Luis Sebastián 
dc.date.accessioned2024-04-02T12:21:50Z
dc.date.available2024-04-02T12:21:50Z
dc.date.issued2015
dc.identifier.citationAdvanced Protocols in Oxidative Stress III. Methods in Molecular Biology, vol 1208, pp. 123-138, 2015es_ES
dc.identifier.urihttp://hdl.handle.net/10835/16245
dc.description.abstractOxidative stress arises when the antioxidant capacity of cells to clean the excess production of reactive oxygen species (ROS) decreases. Several human diseases seem to be related with an increment in the oxidative stress. In this regard, GSH present in the cells works by neutralizing ROS and other xenobiotics through the glutathione S-transferase (GST) enzyme. Thus, the level of expression of GST is an important factor in determining the sensitivity of cells to toxic chemicals or xenobiotic compounds. Therefore, the detection of GST levels is fundamental in the clinical diagnosis of ROS-related diseases. Here, we describe a methodology, based on the voltammetric properties of the ferrocene group (used as electrochemical probe), which can be applied for selective detection of GST levels in human cells. The electrochemical signal measured is associated to the specific interaction of a ferrocenyl-GSH derivate with the G- and H-sites of this enzyme.es_ES
dc.language.isoenes_ES
dc.publisherHumana Press, Springeres_ES
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectFerrocene–glutathione conjugateses_ES
dc.subjectBindinges_ES
dc.subjectVoltammetryes_ES
dc.subjectElectrochemical sensorses_ES
dc.subjectGlutathione S-transferasees_ES
dc.titleElectrochemical detection of glutathione S-transferase: An important enzyme in the cell protective mechanism against oxidative stresses_ES
dc.typeinfo:eu-repo/semantics/bookes_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES
dc.relation.projectIDCTQ 2010-17848, CVI-6028, FQM-6903es_ES


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Attribution-NonCommercial-NoDerivatives 4.0 Internacional
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