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Targeted mass spectrometry analysis of Clostridium perfringens toxins

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F19%3A00537016" target="_blank" >RIV/60162694:G44__/19:00537016 - isvavai.cz</a>

  • Alternative codes found

    RIV/60162694:G33__/19:N0000006 RIV/62690094:18470/19:50015557

  • Result on the web

    <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6468457/" target="_blank" >https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6468457/</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/toxins11030177" target="_blank" >10.3390/toxins11030177</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Targeted mass spectrometry analysis of Clostridium perfringens toxins

  • Original language description

    Targeted proteomics recently proved to be a technique for the detection and absolute quantification of proteins not easily accessible to classical bottom-up approaches. Due to this, it has been considered as a high fidelity tool to detect potential warfare agents in wide spread kinds of biological and environmental matrices. Clostridium perfringens toxins are considered to be potential biological weapons, especially the epsilon toxin which belongs to a group of the most powerful bacterial toxins. Here, the development of a target mass spectrometry method for the detection of C. perfringens protein toxins (alpha, beta, beta2, epsilon, iota) is described. A high-resolution mass spectrometer with a quadrupole-Orbitrap system operating in target acquisition mode (parallel reaction monitoring) was utilized. Because of the lack of commercial protein toxin standards recombinant toxins were prepared within Escherichia coli. The analysis was performed using proteotypic peptides as the target compounds together with their isotopically labeled synthetic analogues as internal standards. Calibration curves were calculated for each peptide in concentrations ranging from 0.635 to 1101 fmol/mu L. Limits of detection and quantification were determined for each peptide in blank matrices.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    30108 - Toxicology

Result continuities

  • Project

    <a href="/en/project/VH20172020012" target="_blank" >VH20172020012: Preparation of the collection of biologically significant toxins with the support of European biological European biodefence laboratory network</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2019

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Toxins

  • ISSN

    2072-6651

  • e-ISSN

    2072-6651

  • Volume of the periodical

    11

  • Issue of the periodical within the volume

    3

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    18

  • Pages from-to

    177

  • UT code for WoS article

    000464472400001

  • EID of the result in the Scopus database

    2-s2.0-85063712474