Citlivé stanovení organofosfátů ve vodách prostřednictvím piezoelektrického biosensoru
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F05%3A00014127" target="_blank" >RIV/00216224:14310/05:00014127 - isvavai.cz</a>
Výsledek na webu
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DOI - Digital Object Identifier
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Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Sensitive detection of organophosphates in river water by means of a piezoelectric biosensor
Popis výsledku v původním jazyce
A highly sensitive piezoelectric biosensor has been developed for detection of cholinesterase inhibitors.The inhibitor benzoylecgonine-1,8-diamino-3,4-dioxaoctane(BZE-DADOO) was immobilized on a monolayer of 11-mercaptomonoundecanoic acid (MUA) selfassembled on the gold surface of the sensor. The binding of high-molecular-weight cholinesterase to the immobilized cocaine derivative was monitored with a mass sensitive piezoelectric quartz crystal (quartz crystal nanobalance; QCN). In the presence of an inhibiting substance in the sample, the binding of cholinesterase to the immobilized inhibitor was reduced. The decrease of the rate of mass change was proportional to the concentration of free inhibitor in the sample. This way the affinity sensor followedanti-cholinesterase toxicity and the enzyme activity of ChE was not addressed. An assay for detection of organophosphates (OP) was optimized. Regeneration of the sensor surface was achieved with 1 mol/L formic acid, which enabled 40 meas
Název v anglickém jazyce
Sensitive detection of organophosphates in river water by means of a piezoelectric biosensor
Popis výsledku anglicky
A highly sensitive piezoelectric biosensor has been developed for detection of cholinesterase inhibitors.The inhibitor benzoylecgonine-1,8-diamino-3,4-dioxaoctane(BZE-DADOO) was immobilized on a monolayer of 11-mercaptomonoundecanoic acid (MUA) selfassembled on the gold surface of the sensor. The binding of high-molecular-weight cholinesterase to the immobilized cocaine derivative was monitored with a mass sensitive piezoelectric quartz crystal (quartz crystal nanobalance; QCN). In the presence of an inhibiting substance in the sample, the binding of cholinesterase to the immobilized inhibitor was reduced. The decrease of the rate of mass change was proportional to the concentration of free inhibitor in the sample. This way the affinity sensor followedanti-cholinesterase toxicity and the enzyme activity of ChE was not addressed. An assay for detection of organophosphates (OP) was optimized. Regeneration of the sensor surface was achieved with 1 mol/L formic acid, which enabled 40 meas
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CE - Biochemie
OECD FORD obor
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Návaznosti výsledku
Projekt
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Návaznosti
Z - Vyzkumny zamer (s odkazem do CEZ)
Ostatní
Rok uplatnění
2005
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Analytical and Bioanalytical Chemistry
ISSN
1618-2642
e-ISSN
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Svazek periodika
382
Číslo periodika v rámci svazku
5
Stát vydavatele periodika
CZ - Česká republika
Počet stran výsledku
7
Strana od-do
1904-1911
Kód UT WoS článku
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EID výsledku v databázi Scopus
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