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Superficially bound acetylcholinesterase based on a chitosan matrix for neurotoxiccCompound assay by a photographic technique

Identifikátory výsledku

  • Kód výsledku v IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F18%3A43889485" target="_blank" >RIV/60162694:G44__/18:43889485 - isvavai.cz</a>

  • Výsledek na webu

    <a href="https://www.tandfonline.com/doi/abs/10.1080/00032719.2017.1381846?journalCode=lanl20" target="_blank" >https://www.tandfonline.com/doi/abs/10.1080/00032719.2017.1381846?journalCode=lanl20</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1080/00032719.2017.1381846" target="_blank" >10.1080/00032719.2017.1381846</a>

Alternativní jazyky

  • Jazyk výsledku

    angličtina

  • Název v původním jazyce

    Superficially bound acetylcholinesterase based on a chitosan matrix for neurotoxiccCompound assay by a photographic technique

  • Popis výsledku v původním jazyce

    Smartphones have become popular in the last decade and they have been used in analytical chemistry as easy detection systems with comparable parameters to standard laboratory equipment. This work focuses on the attachment of enzyme acetylcholinesterase on the previously activated chitosan. Acetylcholine splits the neurotransmitter acetylcholine, as a natural substrate, into choline and acetic acid. However, this compound can cleave alternative substrates, e.g., indoxyl acetate, which was used in this work. The conversion of the substrate is blocked or slowed down by inhibitors from which galantamine and tacrine were tested as model inhibitors with detection limits of 1.1 and 0.18 mu M, respectively. The measurement procedure was performed on a three-dimensional printed holder and red-green-blue channels were used for digital photography evaluation. The method was validated using a standard Ellman&apos;s spectrophotometric assay. We successfully attached acetylcholinesterase on the chitosan surface that was used for the inhibitor assay. The long-term stability of the immobilized enzyme as well as the sensitivity to organic solvents were also tested. The proposed method appeared to be suitable for the rapid and inexpensive assay of neurotoxic compounds.

  • Název v anglickém jazyce

    Superficially bound acetylcholinesterase based on a chitosan matrix for neurotoxiccCompound assay by a photographic technique

  • Popis výsledku anglicky

    Smartphones have become popular in the last decade and they have been used in analytical chemistry as easy detection systems with comparable parameters to standard laboratory equipment. This work focuses on the attachment of enzyme acetylcholinesterase on the previously activated chitosan. Acetylcholine splits the neurotransmitter acetylcholine, as a natural substrate, into choline and acetic acid. However, this compound can cleave alternative substrates, e.g., indoxyl acetate, which was used in this work. The conversion of the substrate is blocked or slowed down by inhibitors from which galantamine and tacrine were tested as model inhibitors with detection limits of 1.1 and 0.18 mu M, respectively. The measurement procedure was performed on a three-dimensional printed holder and red-green-blue channels were used for digital photography evaluation. The method was validated using a standard Ellman&apos;s spectrophotometric assay. We successfully attached acetylcholinesterase on the chitosan surface that was used for the inhibitor assay. The long-term stability of the immobilized enzyme as well as the sensitivity to organic solvents were also tested. The proposed method appeared to be suitable for the rapid and inexpensive assay of neurotoxic compounds.

Klasifikace

  • Druh

    J<sub>imp</sub> - Článek v periodiku v databázi Web of Science

  • CEP obor

  • OECD FORD obor

    10406 - Analytical chemistry

Návaznosti výsledku

  • Projekt

  • Návaznosti

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Ostatní

  • Rok uplatnění

    2018

  • Kód důvěrnosti údajů

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

Údaje specifické pro druh výsledku

  • Název periodika

    Analytical Letters

  • ISSN

    0003-2719

  • e-ISSN

  • Svazek periodika

    51

  • Číslo periodika v rámci svazku

    10

  • Stát vydavatele periodika

    US - Spojené státy americké

  • Počet stran výsledku

    11

  • Strana od-do

    1622-1632

  • Kód UT WoS článku

    000429348300013

  • EID výsledku v databázi Scopus

    2-s2.0-85044085562