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Statements

Subject Item
n2:RIV%2F00216275%3A25310%2F09%3A00008364%21RIV10-MSM-25310___
rdf:type
n15:Vysledek skos:Concept
dcterms:description
Kinetic evidence has indicated that methanolysis of synthesized 4-acetoxybenzyl carbamates proceeds via a one-step (concerted) mechanism. Concerted 1,6-elimination produces the very reactive 1,4-quinonemethide, which was trapped in the form of 4-methoxymethylphenol. The inhibition activity of benzyl N-phenylcarbamates to acetylcholinesterase (ACHE) and butyrylcholinesterase (BCHE) was also tested. The found IC50 values varied within the limits of 199-535 mu mol.l(-1) for ACHE and 21-177 mu mol.l(-1) for BCHE. The found values of partition coefficient (P-ow) in the range of 1.5-11.5 represent a prerequisite of good transport of benzyl N-phenylcarbamates through haemato-encephalic barrier. Kinetic evidence has indicated that methanolysis of synthesized 4-acetoxybenzyl carbamates proceeds via a one-step (concerted) mechanism. Concerted 1,6-elimination produces the very reactive 1,4-quinonemethide, which was trapped in the form of 4-methoxymethylphenol. The inhibition activity of benzyl N-phenylcarbamates to acetylcholinesterase (ACHE) and butyrylcholinesterase (BCHE) was also tested. The found IC50 values varied within the limits of 199-535 mu mol.l(-1) for ACHE and 21-177 mu mol.l(-1) for BCHE. The found values of partition coefficient (P-ow) in the range of 1.5-11.5 represent a prerequisite of good transport of benzyl N-phenylcarbamates through haemato-encephalic barrier.
dcterms:title
Substituted benzyl N-phenylcarbamates - their solvolysis and inhibition activity to acetylcholinesterase and butyrylcholinesterase Substituted benzyl N-phenylcarbamates - their solvolysis and inhibition activity to acetylcholinesterase and butyrylcholinesterase
skos:prefLabel
Substituted benzyl N-phenylcarbamates - their solvolysis and inhibition activity to acetylcholinesterase and butyrylcholinesterase Substituted benzyl N-phenylcarbamates - their solvolysis and inhibition activity to acetylcholinesterase and butyrylcholinesterase
skos:notation
RIV/00216275:25310/09:00008364!RIV10-MSM-25310___
n3:aktivita
n8:Z
n3:aktivity
Z(MSM0021627501), Z(MSM0021627502)
n3:cisloPeriodika
7
n3:dodaniDat
n14:2010
n3:domaciTvurceVysledku
n7:6034543 n7:2747472 n7:1357727 n7:6973442 n7:4978684
n3:druhVysledku
n10:J
n3:duvernostUdaju
n6:S
n3:entitaPredkladatele
n11:predkladatel
n3:idSjednocenehoVysledku
344640
n3:idVysledku
RIV/00216275:25310/09:00008364
n3:jazykVysledku
n17:eng
n3:klicovaSlova
carbamates; acetylcholinesterase; 1; 4-quinonemethide; inhibition
n3:klicoveSlovo
n9:4-quinonemethide n9:carbamates n9:inhibition n9:acetylcholinesterase n9:1
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[54C81E2D3EA6]
n3:nazevZdroje
ARKIVOC
n3:obor
n18:CC
n3:pocetDomacichTvurcuVysledku
5
n3:pocetTvurcuVysledku
5
n3:rokUplatneniVysledku
n14:2009
n3:svazekPeriodika
-
n3:tvurceVysledku
Štěpánková, Šárka Drabina, Pavel Čegan, Alexander Sedlák, Miloš Hanusek, Jiří
n3:zamer
n13:MSM0021627501 n13:MSM0021627502
s:issn
1424-6376
s:numberOfPages
11
n16:organizacniJednotka
25310