scholarly journals <em>In vitro</em> reactivation of chlorpyrifos-inhibited rat brain acetylcholinesterase from pyrazole-oxime derivatives

2020 ◽  
Author(s):  
Manjunath Katagi ◽  
Girish Bolakatti ◽  
Sujatha ML ◽  
Suchitra M ◽  
Shivlingrao Mamledesai
Keyword(s):  
Rat Brain ◽  
Oxime Derivatives ◽  
Brain Acetylcholinesterase

KA-672 inhibits rat brain acetylcholinesterase in vitro but not in vivo

1999 ◽  
Vol 263 (2-3) ◽  
pp. 193-196 ◽  
Author(s):  
Michael Hilgert ◽  
Michael Nöldner ◽  
Shyam S Chatterjee ◽  
Jochen Klein
Keyword(s):  
Rat Brain ◽  
Brain Acetylcholinesterase

In vitro Reactivation of Chlorpyrifos-inhibited Rat Brain Acetylcholinesterase from 2-Quinolone Substituted Thiazole derivatives

2014 ◽  
Vol 4 (2) ◽  
pp. 57-61
Author(s):  
Manjunatha S. Katagi ◽  
Jennifer Fernandes ◽  
Darbhamulla Satyanarayana ◽  
Girish Bolakatti ◽  
Shivalingrao NagabhushanMamle
Keyword(s):  
Rat Brain ◽  
Thiazole Derivatives ◽  
Brain Acetylcholinesterase

Ethidium bromide inhibits rat brain acetylcholinesterase activity in vitro

2006 ◽  
Vol 162 (2) ◽  
pp. 121-127 ◽  
Author(s):  
Cinthia M. Mazzanti ◽  
Roselia M. Spanevello ◽  
Adriana Obregon ◽  
Luciane B. Pereira ◽  
Cristiane A. Streher ◽  
...  
Keyword(s):  
Rat Brain ◽  
Ethidium Bromide ◽  
Acetylcholinesterase Activity ◽  
Brain Acetylcholinesterase

Kinetics of inhibition of acetylcholinesterase by 9-hydrazino-1,2,3,4-tetrahydroacridine and 9-amino-10-methyl-1,2,3,4-tetrahydroacridinium in vitro

1980 ◽  
Vol 45 (3) ◽  
pp. 966-976 ◽  
Author(s):  
Jiří Patočka ◽  
Jiří Bajgar ◽  
Jiří Bielavský
Keyword(s):  
Rat Brain ◽  
Active Center ◽  
Active Surface ◽  
Competitive Inhibitor ◽  
Inhibitory Effect ◽  
Inhibitor Molecule ◽  
Hydrophobic Domain ◽  
Noncompetitive Inhibitor ◽  
Brain Acetylcholinesterase

The kinetics was studied of the inhibition of solubilized rat brain acetylcholinesterase by 9-hydrazino-1,2,3,4-terahydroacridine (THH) and 9-amino-10-methyl-1,2,3,4-tetrahydroacridinium (QTHA); the inhibitory effect was compared with the effect of tacrine (9-amino-1,2,3,4-tetrahydroacridine, THA). It was observed that THH is a reversible, noncompetitive inhibitor of rat brain acetylcholinesterase (Ki = 0.16 μM) and that it binds, similarly to THA, to the hydrophobic domain of the active center of acetylcholinesterase thus simultaneously inhibiting the formation of complex ES2 with acetylcholine as substrate. This eliminates the inhibition of acetylcholinesterase by an excess of substrate. QTHA is a mixed, competitive-non-competitive inhibitor characterized by KI comp = 5.3 μM and Ki noncomp = 0.08 μM. QTHA binds to an entirely different site of the active surface of acetylcholinesterase than THA and THH. This binding site is most likely the so-called β-anionic or also peripheric anionic site to which, e.g. atropine is also bound. Both inhibitors studied form with acetylcholinesterase a reversible, enzymatically inactive complex in which one inhibitor molecule is bonded to each active center of the enzyme.

In vitro investigation of efficacy of new reactivators on OPC inhibited rat brain acetylcholinesterase

2013 ◽  
Vol 203 (1) ◽  
pp. 139-143 ◽  
Author(s):  
Vasil N. Atanasov ◽  
Iskra Petrova ◽  
Christophor Dishovsky
Keyword(s):  
Rat Brain ◽  
In Vitro Investigation ◽  
Brain Acetylcholinesterase
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