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Interactions of the Organophosphates Paraoxon and Methyl Paraoxon with Mouse Brain Acetylcholinesterase [PDF]

Toxicological Sciences, 2000
The mechanism of acute toxicity of the organophosphorus insecticides has been known for many years to be inhibition of the critical enzyme acetylcholinesterase (EC 3.1.1.7), with the resulting excess acetylcholine accumulation leading to symptoms of cholinergic excess.
S A, Kardos, L G, Sultatos
exaly   +3 more sources

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Paraoxon reversibly inhibits neurotoxic esterase

Toxicology and Applied Pharmacology, 1985
It has recently been reported that two paraoxon-insensitive carboxylesterases may be distinguished by their sensitivity to mipafox. However, we have not been able to reliably detect two components under the conditions of the widely used assay for neurotoxic esterase (NTE).
C D, Carrington, M B, Abou-Donia
openaire   +2 more sources

Hydrolysis of Paraoxon in Mammalian Blood

Nature, 1961
SEVERAL publications have indicated that in the detoxication of paraoxon (diethyl p-nitrophenyl phosphate, ‘E600,’ ‘Mintacol’) the mammalian blood serum might be of importance1–3. Aldridge4 was first to describe the existence of an A esterase (aryl-, aromatic esterase) which hydrolyses paraoxon.
E G, ERDOS, L E, BOGGS
exaly   +3 more sources

Paraoxon Sensitive Phenylvalerate Hydrolase in Assessing the Severity of Acute Paraoxon Poisoning

Journal of Toxicology: Clinical Toxicology, 2001
Intoxications with organophosphorous compounds, especially paraoxon, are frequent. Organophosphorous compounds inhibit serine hydrolases such as acetylcholine, butyrilcholine, and carboxyl esterases although acetylcholine and butyrylcholine are too sensitive to paraoxon to be useful markers of severity.
G, Petroianu, B, Kärcher, N, Kern, W, Bergler, R, Rüfer   +4 more
openaire   +2 more sources

PARAOXON HYDROLYSIS VS. COVALENT BINDING IN THE ELIMINATION OF PARAOXON IN THE RABBIT

Drug Metabolism and Disposition, 1985
Hydrolysis and covalent binding to nonessential esterases are two biochemical processes which can prevent paraoxon from reacting with the essential enzyme, acetylcholinesterase. Both processes have been proposed as the primary route of paraoxon detoxification in vivo.
E G, Butler, H W, Eckerson, B N, La Du
openaire   +2 more sources

Phosphotriesterase Decreases Paraoxon Toxicity in Mice

Toxicology and Applied Pharmacology, 1993
The effect of phosphotriesterase (PTE) on the ip toxicity of paraoxon was studied in mice. The PTE preparation (0.1 ml; paraoxon-hydrolyzing activity, 1.5 mumol/min) was given iv. Cholinesterase activities were measured 2 hr after paraoxon administration.
E, Kaliste-Korhonen, P, Ylitalo, O, Hänninen, F M, Raushel   +3 more
openaire   +2 more sources

Mechanism Underlying Organophosphate Paraoxon-Induced Kinetic Tremor

Neurotoxicity Research, 2019
Organophosphates (OPs) inhibit cholinesterase and hyperactivate the acetylcholinergic nervous system in the brain, causing motor disorders (e.g., tremor and seizures). Here, we performed behavioral and immunohistochemical studies in mice and rats to investigate the tremorgenic mechanism of paraoxon, an active metabolite of parathion.
Higor Alves Iha, Naofumi Kunisawa, Saki Shimizu, Misaki Onishi, Yuji Nomura, Nami Matsubara, Chihiro Iwai, Mizuki Ogawa, Mai Hashimura, Kazuaki Sato, Masaki Kato, Yukihiro Ohno   +11 more
openaire   +2 more sources

Loss of paraoxon in aqueous acetonitrile extractions

Bulletin of Environmental Contamination and Toxicology, 1977
There are many methods available for the extraction.of parathion from diverse substrates for residue analysis, among which is a method wherein the pesticide is partitioned from an acetonit r i l e extract after i t has been diluted with water. Finley and co-workers (FINLEY and ROGILLIO, 1969, FINLEY, et al .
H R, McLean, S, Futagaki, J T, Leffingwell   +2 more
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Rat liver paraoxonase (paraoxon arylesterase)

Pesticide Biochemistry and Physiology, 1984
Abstract Paraoxonase in the liver of male Sprague-Dawley rats was studied by using [ phenyl -1- 14 C]paraoxon. Examination of the enzyme activity in subcellular fractions of liver homogenates indicated that hepatic paraoxonase is essentially a microsomal enzyme with a pH optimum of 7.5 to 7.8.
Jane E. McIlvain, Julita Timoszyk, Tsutomu Nakatsugawa   +2 more
openaire   +1 more source

Paraoxon inhibition of an insect egg lipase

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1971
Abstract A lipase present in an insect egg ( Diabrotica undecimpunctata howardi Barber) is sensitive to inhibition by low concentrations (approx. 10 −6 M) of diethyl- p -nitrophenyl phosphate. The inhibition occurs only in the presence of substrate; i.e. , exposure of the enzyme to inhibitor in the absence of substrate does not result in inhibition.
J L, Krysan, P L, Guss
openaire   +2 more sources