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| Description
| - Kinetic parameters were evaluated for inhibition of native and reactivation of tabun-inhibited human erythrocyte acetylcholinesterase (AChE; EC 3.1.1.7) and human plasma butyrylcholinesterase (BChE; EC 3.1.1.8) by three bispyridinium para-aldoximes with butane (K074), but-2-ene (K075) or xylene-like linker (K114). Tested aldoximes reversibly inhibited both cholinesterases with the preference for binding to the native AChE. Both cholinesterases showed the highest affinity for K114 (Ki was 0.01 mM for AChE and 0.06 mM for BChE). The reactivation of tabun-inhibited AChE was efficient by K074 and K075. Their overall reactivation rate constants were around 2000 min-1M-1, which is seven times higher than for the classical bispyridinium para-aldoxime TMB-4. The reactivation of tabun-inhibited AChE assisted by K114 was slow and reached 90 % after 20 h. Since the aldoxime binding affinity of tabun-inhibited AChE was similar for all tested aldoximes (and corresponded to their Ki), the rate of the nucleophilic d
- Kinetic parameters were evaluated for inhibition of native and reactivation of tabun-inhibited human erythrocyte acetylcholinesterase (AChE; EC 3.1.1.7) and human plasma butyrylcholinesterase (BChE; EC 3.1.1.8) by three bispyridinium para-aldoximes with butane (K074), but-2-ene (K075) or xylene-like linker (K114). Tested aldoximes reversibly inhibited both cholinesterases with the preference for binding to the native AChE. Both cholinesterases showed the highest affinity for K114 (Ki was 0.01 mM for AChE and 0.06 mM for BChE). The reactivation of tabun-inhibited AChE was efficient by K074 and K075. Their overall reactivation rate constants were around 2000 min-1M-1, which is seven times higher than for the classical bispyridinium para-aldoxime TMB-4. The reactivation of tabun-inhibited AChE assisted by K114 was slow and reached 90 % after 20 h. Since the aldoxime binding affinity of tabun-inhibited AChE was similar for all tested aldoximes (and corresponded to their Ki), the rate of the nucleophilic d (en)
- Byly zhodnoceny kinetické parametry pro inhibici nativní a reaktivaci tabunem inhibované erythrocytární acetylcholinesterázy (AChE; EC 3.1.1.7) a lidské plasmatické butyrylcholinesterázy (BChE; EC 3.1.1.8) se třemi bispyridiniovými para-aldoximy s butanem (K074), but-2-enem (K075) či xylenovým (K114) spojovacím řetězcem.Testované aldoximy reversibilně inhibovaly obě cholinesterázy s preferencí vázat se na nativní AChE. Obě cholinesterázy prokázaly nejvyšší afinitu pro K114 (Ki byla 0.01 mM pro AChE a 0.06 mM pro BChE). Reaktivace tabunem-inhibované AChE byla účiná pro K074 a K075. Jejich celkové reaktivační konstanty byly kolem 2000 min-1M-1,které jsou sedmkrát vyšší než pro klasický bispyridiniový para-aldoxim TMB-4. Reaktivace tabunem-inhibované AChE pomocí K114 byla pomalá a dosáhla 90% po 20 hodinách. Ačkoliv vazebná afinita aldoximu k tabunem-inhibované AChE byla stejná pro všechny testované aldoximy (a shodující se s jejich Ki), rychlost nukleofilního odstranění fosforylové skupiny ze serinu v a (cs)
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| Title
| - Interactions of butane, but-2-ene or xylene-like linked bispyridinium para-aldoximes with native and tabun-inhibited human cholinesterases
- Interactions of butane, but-2-ene or xylene-like linked bispyridinium para-aldoximes with native and tabun-inhibited human cholinesterases (en)
- Interakce bispyridiniových para-aldoximu spojených butanem, bute-2-enem či xylenem s nativním a tabunem-inhibovanou lidskou cholinesterázou (cs)
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| skos:prefLabel
| - Interactions of butane, but-2-ene or xylene-like linked bispyridinium para-aldoximes with native and tabun-inhibited human cholinesterases
- Interactions of butane, but-2-ene or xylene-like linked bispyridinium para-aldoximes with native and tabun-inhibited human cholinesterases (en)
- Interakce bispyridiniových para-aldoximu spojených butanem, bute-2-enem či xylenem s nativním a tabunem-inhibovanou lidskou cholinesterázou (cs)
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| skos:notation
| - RIV/60162694:G44__/08:00001975!RIV09-MO0-G44_____
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| http://linked.open...avai/riv/aktivita
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| http://linked.open...avai/riv/aktivity
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| http://linked.open...iv/cisloPeriodika
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| http://linked.open...vai/riv/dodaniDat
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| http://linked.open...aciTvurceVysledku
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| http://linked.open.../riv/druhVysledku
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| http://linked.open...iv/duvernostUdaju
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| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
| |
| http://linked.open...ai/riv/idVysledku
| - RIV/60162694:G44__/08:00001975
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| http://linked.open...riv/jazykVysledku
| |
| http://linked.open.../riv/klicovaSlova
| - Acetylcholinesterase; Butyrylcholinesterase; Nerve Agents; Oxime; Protection; Reactivation (en)
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| http://linked.open.../riv/klicoveSlovo
| |
| http://linked.open...odStatuVydavatele
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| http://linked.open...ontrolniKodProRIV
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| http://linked.open...i/riv/nazevZdroje
| - Chemico-Biological Interactions
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| http://linked.open...in/vavai/riv/obor
| |
| http://linked.open...ichTvurcuVysledku
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| http://linked.open...cetTvurcuVysledku
| |
| http://linked.open...UplatneniVysledku
| |
| http://linked.open...v/svazekPeriodika
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| http://linked.open...iv/tvurceVysledku
| - Kuča, Kamil
- Bosak, A.
- Kovarik, Z.
- Calic, M.
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| http://linked.open...ain/vavai/riv/wos
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| http://linked.open...n/vavai/riv/zamer
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| issn
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| number of pages
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| http://localhost/t...ganizacniJednotka
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