About: Kinetics of In Vitro Inhibition of Acetylcholinesterase by Nineteen New Carbamates     Goto   Sponge   NotDistinct   Permalink

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  • Two series A and B of 12 and 7 new carbamate derivates were tested in vitro as acetylcholinesterase inhibitors. The tests were performed in the batch stirred reactor at 25°C, pH 8, ionic strength 0.11 M and catalytic activity of the enzyme preparation 0.14 U mL-1 of the reaction mixture. The temporal dependences of actual concentrations of acetylcholine, choline and acetic acid were determined by two independent analytical methods, HPLC and pH-stat. For all used inhibitors, the model of competitive irreversible inhibition was valid. The inhibition rate constant k3 and qualified estimation of the absolute acetylcholinesterase concentration in the reaction mixture were calculated. The partition coefficients Kow between n-octanol and water of all used inhibitors were determined. The k3 and Kow values were correlated with the Hammett and Hansch substituent constants and with the calculated docking and binding energies of the reaction between the tested inhibitors and acetylcholinesterase.
  • Two series A and B of 12 and 7 new carbamate derivates were tested in vitro as acetylcholinesterase inhibitors. The tests were performed in the batch stirred reactor at 25°C, pH 8, ionic strength 0.11 M and catalytic activity of the enzyme preparation 0.14 U mL-1 of the reaction mixture. The temporal dependences of actual concentrations of acetylcholine, choline and acetic acid were determined by two independent analytical methods, HPLC and pH-stat. For all used inhibitors, the model of competitive irreversible inhibition was valid. The inhibition rate constant k3 and qualified estimation of the absolute acetylcholinesterase concentration in the reaction mixture were calculated. The partition coefficients Kow between n-octanol and water of all used inhibitors were determined. The k3 and Kow values were correlated with the Hammett and Hansch substituent constants and with the calculated docking and binding energies of the reaction between the tested inhibitors and acetylcholinesterase. (en)
Title
  • Kinetics of In Vitro Inhibition of Acetylcholinesterase by Nineteen New Carbamates
  • Kinetics of In Vitro Inhibition of Acetylcholinesterase by Nineteen New Carbamates (en)
skos:prefLabel
  • Kinetics of In Vitro Inhibition of Acetylcholinesterase by Nineteen New Carbamates
  • Kinetics of In Vitro Inhibition of Acetylcholinesterase by Nineteen New Carbamates (en)
skos:notation
  • RIV/00216275:25310/11:39895922!RIV13-MSM-25310___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • S, Z(MSM0021627501), Z(MSM0021627502)
http://linked.open...iv/cisloPeriodika
  • 4
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 207420
http://linked.open...ai/riv/idVysledku
  • RIV/00216275:25310/11:39895922
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • docking energies; HPLC; kinetics; inhibition; carbamates; acetylcholinesterase; in vitro; enzymatic; hydrolysis; Acetylcholine (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • NL - Nizozemsko
http://linked.open...ontrolniKodProRIV
  • [E11956F65797]
http://linked.open...i/riv/nazevZdroje
  • Current Enzyme Inhibition
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 7
http://linked.open...iv/tvurceVysledku
  • Pařík, Patrik
  • Čegan, Alexander
  • Khan, Mahmud T.H.
  • Komers, Karel
  • Kovářová, Markéta
  • Zatloukalová, Martina
http://linked.open...n/vavai/riv/zamer
issn
  • 1573-4080
number of pages
http://bibframe.org/vocab/doi
  • 10.2174/157340811799860560
http://localhost/t...ganizacniJednotka
  • 25310
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