About: Reactivation of human brain homogenate cholinesterases inhibited by tabun using newly developed oximes K117 and K127     Goto   Sponge   NotDistinct   Permalink

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Description
  • Newly developed acetylcholinesterase reactivators K117 [1,5-bis(4-hydroxyiminomethylpyridinium)-3-oxapentane dichloride] and K127 [(1-(4-hydroxyiminomethylpyridinium)-5-(4-carbamoylpyridinium)-3-oxapentane dibromide)] were tested for their potency to reactivate tabun-inhibited human brain cholinesterases. Pralidoxime and trimedoxime were chosen as standard reference reactivators. Human tissue was used, as that was closer on the real treatment of human beings. As a result, oxime K127 was found as the best tested reactivator according to the constant k(r), characterizing the overall reactivation process. On the contrary, the maximal reactivation ability expressed as percentage of reactivation was the best for trimedoxime. This differences were caused as a result of using the enzyme from different species. Due to this, experiments on human tissue should be conducted after in vitro and in vivo tests on animals to eliminate such important failures of promising oximes.
  • Newly developed acetylcholinesterase reactivators K117 [1,5-bis(4-hydroxyiminomethylpyridinium)-3-oxapentane dichloride] and K127 [(1-(4-hydroxyiminomethylpyridinium)-5-(4-carbamoylpyridinium)-3-oxapentane dibromide)] were tested for their potency to reactivate tabun-inhibited human brain cholinesterases. Pralidoxime and trimedoxime were chosen as standard reference reactivators. Human tissue was used, as that was closer on the real treatment of human beings. As a result, oxime K127 was found as the best tested reactivator according to the constant k(r), characterizing the overall reactivation process. On the contrary, the maximal reactivation ability expressed as percentage of reactivation was the best for trimedoxime. This differences were caused as a result of using the enzyme from different species. Due to this, experiments on human tissue should be conducted after in vitro and in vivo tests on animals to eliminate such important failures of promising oximes. (en)
Title
  • Reactivation of human brain homogenate cholinesterases inhibited by tabun using newly developed oximes K117 and K127
  • Reactivation of human brain homogenate cholinesterases inhibited by tabun using newly developed oximes K117 and K127 (en)
skos:prefLabel
  • Reactivation of human brain homogenate cholinesterases inhibited by tabun using newly developed oximes K117 and K127
  • Reactivation of human brain homogenate cholinesterases inhibited by tabun using newly developed oximes K117 and K127 (en)
skos:notation
  • RIV/00216208:11160/09:00300505!RIV11-MSM-11160___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(ME 865), S
http://linked.open...iv/cisloPeriodika
  • 3
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
  • 338202
http://linked.open...ai/riv/idVysledku
  • RIV/00216208:11160/09:00300505
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • oxime; reactivator; cholinesterase; nerve agent; tabun; K-oximes; trimedoxime; pralidoxime (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [3CBFCE38E439]
http://linked.open...i/riv/nazevZdroje
  • Basic & Clinical Pharmacology & Toxicology
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 105
http://linked.open...iv/tvurceVysledku
  • Cabal, Jiří
  • Hrabinová, Martina
  • Kuča, Kamil
  • Musílek, Kamil
  • Novotný, Ladislav
  • Pohanka, Miroslav
  • Žďárová Karasová, Jana
  • Jun, Daniel
  • Musilová, Lucie
  • Soukup, Ondřej
  • Jung, Young Sik
http://linked.open...ain/vavai/riv/wos
  • 000268960200009
issn
  • 1742-7835
number of pages
http://localhost/t...ganizacniJednotka
  • 11160
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