The application of capillary electrophoresis, mass spectrometry and Brdicka reaction in human and rabbit metallothioneins analysis

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dc.contributor.authorKepinska, Martacs
dc.contributor.authorKřížková, Soňacs
dc.contributor.authorGuszpit, Ewelinacs
dc.contributor.authorMerlos Rodrigo, Miguel Ángelcs
dc.contributor.authorMilnerowicz, Halinacs
dc.coverage.issue11cs
dc.coverage.volume27cs
dc.date.issued2018-11-30cs
dc.description.abstractBackground. Metallothioneins (MTs) constitute a family of evolutionary conserved low molecular weight proteins with small variations in their amino acid sequences. They play a role in the regulation of trace metals metabolism, in the detoxification of heavy metal ions and in mechanisms controlling growth, differentiation and proliferation of cells. Objectives. The aim of this study was to evaluate the human and rabbit MTs purity and characterization using advanced analytical approaches. Due to the common use of MT from rabbit liver as a model protein, the properties of the rabbit and human MTs were compared. Material and methods. Capillary electrophoresis (CE), matrix-assisted laser desorption and ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and Brdicka reaction were used for human and rabbit MTs characterization. Results. In chip CE analysis, changes in the range of 5-8 kDa corresponding to the MT monomer, as well as some peaks of 13-14 kDa corresponding to dimers in both species, were observed. Using MALDI-MS, rabbit (MT-2D) and human (MT-1A, MT-1G, MT-1G + Cd and MT-2A) MTs were identified. In the Brdicka reaction analysis, a lower concentration of MTs from both organisms coincided with a decrease in the signal corresponding to MT level (Cat2). However, human MT gave higher Cat2 peak than the same concentration (0.025 mg/mL) of rabbit MT. Conclusions. The applied methods allowed for the characterization of MTs and gave complementary information about MT isoforms. Altered electrochemical activity of human and rabbit MTs, despite the same number of -sulfhydryl (-SH) groups, was observed, which may be due to different availability of MT cysteinyl groups.en
dc.formattextcs
dc.format.extent1601-1608cs
dc.format.mimetypeapplication/pdfcs
dc.identifier.citationAdvances in Clinical and Experimental Medicine. 2018, vol. 27, issue 11, p. 1601-1608.en
dc.identifier.doi10.17219/acem/98916cs
dc.identifier.issn1899-5276cs
dc.identifier.orcid0000-0002-0479-8369cs
dc.identifier.other158025cs
dc.identifier.researcheridE-9617-2012cs
dc.identifier.urihttp://hdl.handle.net/11012/180520
dc.language.isoencs
dc.publisherWroclaw Medical Universitycs
dc.relation.ispartofAdvances in Clinical and Experimental Medicinecs
dc.relation.urihttp://www.advances.umed.wroc.pl/en/article/2018/27/11/1601/cs
dc.rightsCreative Commons Attribution-NonCommercial-NoDerivatives 4.0 Internationalcs
dc.rights.accessopenAccesscs
dc.rights.sherpahttp://www.sherpa.ac.uk/romeo/issn/1899-5276/cs
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/cs
dc.subjectmetallothioneinen
dc.subjectmass spectrometryen
dc.subjectcapillary electrophoresisen
dc.subjectBrdicka reactionen
dc.titleThe application of capillary electrophoresis, mass spectrometry and Brdicka reaction in human and rabbit metallothioneins analysisen
dc.type.driverarticleen
dc.type.statusPeer-revieweden
dc.type.versionpublishedVersionen
sync.item.dbidVAV-158025en
sync.item.dbtypeVAVen
sync.item.insts2025.02.03 15:49:51en
sync.item.modts2025.01.17 16:54:43en
thesis.grantorVysoké učení technické v Brně. Středoevropský technologický institut VUT. Chytré nanonástrojecs
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