The application of capillary electrophoresis, mass spectrometry and Brdicka reaction in human and rabbit metallothioneins analysis
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62156489%3A43210%2F18%3A43914523" target="_blank" >RIV/62156489:43210/18:43914523 - isvavai.cz</a>
Alternative codes found
RIV/00216305:26620/18:PU132950
Result on the web
<a href="http://dx.doi.org/10.17219/acem/98916" target="_blank" >http://dx.doi.org/10.17219/acem/98916</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.17219/acem/98916" target="_blank" >10.17219/acem/98916</a>
Alternative languages
Result language
angličtina
Original language name
The application of capillary electrophoresis, mass spectrometry and Brdicka reaction in human and rabbit metallothioneins analysis
Original language description
Background. 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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
30502 - Other medical science
Result continuities
Project
<a href="/en/project/NV15-28334A" target="_blank" >NV15-28334A: Influence of metallothionein on binding of platinum cytostatics to DNA in cancer cells</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Advances in Clinical and Experimental Medicine
ISSN
1899-5276
e-ISSN
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Volume of the periodical
27
Issue of the periodical within the volume
11
Country of publishing house
PL - POLAND
Number of pages
8
Pages from-to
1601-1608
UT code for WoS article
000451837100020
EID of the result in the Scopus database
2-s2.0-85057861955