The effect of chiral debromoleptophos oxon isomers on acute and delayed neurotoxicity and their inhibitory activity against acetylcholinesterases and neurotoxic esterase

1985 ◽  
Vol 33 (5) ◽  
pp. 884-887 ◽  
Author(s):  
Bryan K. Eya ◽  
T. Roy Fukuto
Keyword(s):  
Inhibitory Activity ◽  
Delayed Neurotoxicity ◽  
Neurotoxic Esterase

scholarly journals Characterization of [3H]di-isopropyl phosphorofluoridate-binding proteins in hen brain. Rates of phosphorylation and sensitivity to neurotoxic and non-neurotoxic organophosphorus compounds

1985 ◽  
Vol 228 (3) ◽  
pp. 537-544 ◽  
Author(s):  
C D Carrington ◽  
M B Abou-Donia
Keyword(s):  
Organophosphorus Compound ◽  
Binding Proteins ◽  
Organophosphorus Compounds ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Reaction Rates ◽  
Binding Activity ◽  
Binding Characteristics ◽  
Delayed Neurotoxicity ◽  
Neurotoxic Esterase

The experiments described in this paper were designed to isolate [3H]di-isopropyl phosphorofluoridate-binding proteins by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis for the purpose of characterizing and identifying potential initiation sites for organophosphorus-compound-induced delayed neurotoxicity. The major Paraoxon-insensitive Mipafox-sensitive binding protein (Mr 160 000) was found to be identical with one previously identified as neurotoxic esterase, an enzyme that has been proposed to be the target site for organophosphorus-compound-induced delayed neurotoxicity. However, two other binding proteins with suitable binding characteristics were also found in smaller amounts, one of which has not been detected previously. Di-isopropyl phosphorofluoridate was found to phosphorylate all three of these proteins at rates similar to the rate at which neurotoxic esterase is inhibited by di-isopropyl phosphorofluoridate. Varying the concentration of di-isopropyl phosphorofluoridate or the time of incubation produced similar increases in binding to each of the labelled proteins. This suggests that the reaction rates of di-isopropyl phosphorofluoridate with proteins may be described by first-order kinetics, and the concentration of the Michael is complex formed during binding is minimal for all the phosphorylated proteins. The recovery of the binding activity in the 160 000-Mr band was found to be similar to the recovery of neurotoxic esterase activity, lending further support to the contention that this band is identical with neurotoxic esterase.

scholarly journals Histochemical demonstration of neurotoxic esterase.

1989 ◽  
Vol 37 (5) ◽  
pp. 589-596 ◽  
Author(s):  
G B Koelle ◽  
N S Thampi ◽  
M S Han ◽  
E J Olajos
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Enzymatic Activity ◽  
Histochemical Demonstration ◽  
The Other ◽  
Delayed Neurotoxicity ◽  
The Central Nervous System ◽  
Cryostat Sections ◽  
Insoluble Precipitate ◽  
Neurotoxic Esterase

We developed a histochemical method for localizing neurotoxic esterase (NTE), defined as the phenylvalerate (PV)-hydrolyzing esterase that is resistant to 40 microM paraoxon (A) but inactivated by paraoxon plus 50 microM mipafox (B). NTE is considered to be the target enzyme in the production of organophosphorus ester-induced delayed neurotoxicity (OPIDN). Cryostat sections were incubated in a medium containing alpha-naphthyl valerate and 6-benzamido-4-methoxy-m-toluidine diazonium chloride (fast violet B) after treatment with the above-mentioned inhibitors, leading to formation of an aqueous insoluble precipitate at sites of enzymatic activity. NTE activity was estimated as staining detectable in A but not in B. In the central nervous system (CNS) of chicken, NTE appeared to be present primarily in the somata of most neurons, but at sites indistinguishable from those of the other inhibitor-resistant and -sensitive alpha-naphthyl valerate-hydrolyzing esterases. It could not be distinguished in the CNS of cat, probably because it constitutes less than 3% of the total PV-hydrolyzing activity in the CNS of that species.

Chemical and biological safety: Biosensors and nanotechnological methods for the detection and monitoring of chemical and biological agents

2002 ◽  
Vol 74 (12) ◽  
pp. 2311-2316 ◽  
Author(s):  
S. Varfolomeyev ◽  
I. Kurockhin ◽  
A. Eremenko ◽  
Elena Efremenko
Keyword(s):  
Chemical Warfare Agents ◽  
Chemical Warfare ◽  
Pathogenic Microorganisms ◽  
Delayed Neurotoxicity ◽  
Qualitative Detection ◽  
Highly Sensitive ◽  
Defense Technology ◽  
Warfare Agents ◽  
Express Methods ◽  
Neurotoxic Esterase

The elaboration of highly sensitive and express methods for quantitative and qualitative detection and monitoring of chemical warfare agents (CWA), organophosphate and carbamate pesticides, compounds with delayed neurotoxicity, and pathogenic microorganisms and viruses is discussed. The application of potentiometric and amperometric biosensors, automatic biosensors discriminating the neurotoxins of different classes, is performed. The information about biosensors detecting the compounds with delayed neurotoxicity through the evaluation of “neurotoxic esterase”activity in the blood is presented. The use of immunochip technology for the detection of pathogenic microorganisms and viruses is demonstrated. The enzymatic methods of destruction of organophosphorus neurotoxins are considered as the base of new defense technology.

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