• Fisheries and Aquatic Sciences
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• v.2 no.2
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• pp.167-171
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• 1999

This study was designed to develop biomarkers of coastal pollution using biochemical indices of flounder (Paralichthys olivaceus) by changes in lactate dehydrogenase (LDH) activity in the serum and cholinesterase activities in brain membranes. For this purpose acetylcholiesterase (AChE) activity, butyrylcholinesterase (BChE) activity, LDH/AChE ratio and LDH/BChE ratio of cultured flounders at 5 different sites on the southern coast of Korea were compared to those of wild flounders caught in the Pohang, eastern coast of Korea as a control group. Relatively high LDH activities were measured in the serum of flounders cultured on the southern coast of Korea (0.101-0.145 unit) than those in the Pohang control group (0.093 unit). AChE activities were significantly low $(about\;10-20\%)$ in brain membranes of cultured flounders compared to those in the Pohang control group. The ratios of LDH/AChE and LDH/BChE were consistently higher $(136-178\%,\; 155-214\%)$ in cultured flounders than those of Pohang control group. Thus, we propose that the ratios of LDH/AChE and LDH/BChE in flounders could be applicable for the diagnosis of marine pollution.

• Archives of Pharmacal Research
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• v.25 no.6
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• pp.817-819
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• 2002

In the course of screening Korean natural products for acetylcholinesterase (AChE) inhibitory activity, it was found that a methanolic extract of the aerial parts of Corydalis incisa (Papaveraceae) showed significant inhibitory effects on AChE. Corynoline isolated from this plant inhibited AChE activity in a dose-dependent manner, and the $IC_{50}$ value of corynoline was $30.6{\;}{\mu}M$. The AChE inhibitory activity of corynoline was reversible and noncompetitive.

• Journal of Environmental Science International
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• v.17 no.12
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• pp.1325-1330
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• 2008

This study was carried out with the detection for multiresidue of the carbamate pesticide such as carbaryl and cabofuran by enzyme-inhibition method. The check time for determination of acetylcholinesterase(AChE) activity was selected at 60 sec. The AChE activity in chicken brain determined by the Ellman's method was $162{\mu}$mol/min/g protein. $I_{50}$ for AChE by carbamate pesticide with wet kit was 0.169mg/L of carbaryl and 0.089mg/L of cabofuran, respectively. The incubation time for enzyme kit with substrate kit was 30min for determination of AChE activity. Enzyme kit with substrate kit was stable at $4^{\circ}C\;and\;25^{\circ}C$ for 5 days. Limit detection concentration of carbaryl with dry kit for AChE was 0.05mg/L. The dry kit such as wet kit applied Enzyme-Inhibition(EI) method with AChE was confirmed the multi residue method to detect the carbamate pesticides.

• Archives of Pharmacal Research
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• v.14 no.4
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• pp.330-335
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• 1991

The effects of physostigmine and neostigmine on the parathin induced toxicity were examined in adult female rats. Physostigmine $(100\;{\mu}g/kg,\;ip)$ or neostigmine $(200\;{\mu}g/kg,\;ip)$ inhibited acetylcholinesterase (AChE) and cholinesterase (ChE) activities in blood, brain and lung when the enzyme activity was measured 30 min after the treatment. At the doses of two carbamates equipotent on brain AChE, neostigmine showed greater inhibition on peripheral AChE/ChE. The enzyme activity returned to normal in 120 min following the carbamates except in the lung of rats treated with neostigmine. Carbamates administered 30 min prior to parathion (2 mg/kg) antagonized the inhibition of AChE/ChE by parathion when the enzyme activity was measured 2 hr following parathion. Neostigmine showed greater protective effect on peripheral AChE/ChE. The effect of either carbamate on AChE/ChE was not significant 2 hr beyond the parathion treatment. Carbamates decreased the mortality of rats challenged with a lethal dose of parathion (4 mg/kg, ip) either when treated alone or in combination with atropine (10 mg/kg, ip). Lethal action of paraoxon (1.5 mg/ks ip), the active metabolite of parathion was also decreased by the carbamate treatment indicating that the protection was not mediated by competitive inhibition of metabolic conversion of parathion to paraoxon. The results suggest that carbamylation of the active sites may not be the sole underlying mechanism of protection provided by the carbamates.

• Korean Journal of Environmental Agriculture
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• v.6 no.2
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• pp.77-83
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• 1987

Present study was carried out to elucidate the effect of phorate (0,0-dietyl S-ethylthiomethyl phosphorodithioate), an organophosphorus insecticide on the acetylcholinesterase(AChE) and cholinesterase(ChE) activity in the chicken brain and plasma. The inhibitory effect of phorate and its metabolites on AChE and ChE activity was also increased in the order of phorate (p=S,S)$(p=S,SO_2)<phoratoxon$ (p=O,S)$(P=O,SO_2)$. Acute oral $LD_{50}$ of phorate was 1.02mg/kg. After oral administration of phorate, the activity of plasma ChE was inhibited more rapidly then that of brain AChE, whereas recovery of plasma ChE activity was more rapid than that of brain AChE activity.

• Journal of the Korean Society of Food Science and Nutrition
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• v.34 no.3
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• pp.427-432
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• 2005

This study was performed to investigate the effect of natural plant extracts on acetylcholinesterase (AChE) activity and the free radical scavenging activity. The methanolic extracts of plants were tested for AChE inhibitory activity using Ellman's colorimetric method in 96-welled microplates and antioxidant activity as the scavenging effect of 1, 1-diphenyl-2-picryl hydrazyl radical (DPPH). The results showed that AChE activities were inhibited (about 20-30%) in whole plant extract of Daucus carota var. sativa, Hypericum erectum and Fragaria yezoensis. AChE activities were inhibited (about 32-34%) in stems extract of Gingko biloba and leaves extract of Rhododendrondron yedoensa var. poukhanense. Fruit extract of Zanthoxylum schinifolium inhibited (about 18%) AChE activity. And the DPPH scavenging effects as antioxidant activity were similar to L-ascorbic acid in whole plant extract of Fragaria yezoensis and fruits extract of Comus officinalis.

• Fisheries and Aquatic Sciences
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• v.7 no.3
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• pp.171-173
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• 2004

Activity of acetylcholinesterase (AChE) is well known as a biomarker of exposure to organophosphate compounds in aquatic organisms. However, the effect of diethyl phthalate (DEP), a widely used plasticizer, on the chance of AChE activity is not yet known. Olive flounder (Paralichthys olivaceus) were exposed to DEP 300 and 1,000 mg DEP/kg b.w. through three times of intraperitoneal injection and effects were assessed in AChE activity of brain, muscle, heart and eyes of the exposed fish. AChE activity in various tissues of flounder was inhibited after exposure to DEP as a concentration-dependent manner, especially in brain, muscle and heart. Among tissues examined, heart is supposed to be a major part of body which is seriously damaged by DEP exposure. It indicates that DEP induces toxic effects in various organs (brain, muscle and heart), and changes of AChE activities. Such changed activities of AChE might be a useful biomarker to assess the impacts induced by phthalate esters including DEP.

• Parasites, Hosts and Diseases
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• v.51 no.4
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• pp.421-426
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• 2013

Several studies have shown the mechanisms and importance of immune responses against Toxoplasma gondii infection and the notable role of cholinesterases in inflammatory reactions. However, the association between those factors has not yet been investigated. Therefore, the aim of this study was to evaluate the acetylcholinesterase (AChE) activity in blood and lymphocytes and the activity of butyrylcholinesterase (BChE) in serum of rats experimentally infected with T. gondii during the acute phase of infection. For that, an in vivo study was performed with evaluations of AChE and BChE activities on days 5 and 10 post-infection (PI). The activity of AChE in blood was increased on day 5 PI, while in lymphocytes its activity was enhanced on days 5 and 10 PI (P<0.05). No significant difference was observed between groups regarding to the activity of BChE in serum. A positive (P<0.01) correlation was observed between AChE activity and number of lymphocytes. The role of AChE as an inflammatory marker is well known in different pathologies; thus, our results lead to the hypothesis that AChE has an important role in modulation of early immune responses against T. gondii infection.

• International Journal of Industrial Entomology and Biomaterials
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• v.1 no.1
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• pp.73-78
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• 2000

We investigated some biochemical properties of acetylcholinesterase (AChE) in the Bombyx mori larval head. 1% Triton X-100 (v/v) was suitable for extracting AChE from the silkworm larval head but 1 M NaCl was not suitable. PAGE analysis showed a single band of AChE that was detected by histochemical staining using acetylthiocholine as a substrate. AChE was also partially purified with Sepharose 6B and DEAE-cellulose column. Finally, the specific activity of partially purified enzyme solution was 7.6. The study on inhibitor specificity indicated that the enzyme under study was a true cholinesterase (ChE) or AChE. AChE activity was maximum at the substrate concentration of $5{\times}10^{-4}$ M and the excess substrate inhibited the AChE activity. The optimal pH and temperature were pH 7.0-9.0 and 30-35$^{\circ}C$.

• Applied Biological Chemistry
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• v.29 no.3
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• pp.324-330
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• 1986

The responses of brain acetylcholinesterase(Ach-E) and plasma cholinesterase (Ch-E) activities were studied in chicknes given oral doses of Terbufos(S-tert-butyl thiomethyl 0,0-diethyl phosphorodithioate), an organophosphorus insecticide. The acute oral $LD_{50}$ of terbufos was 1.82mg/kg. The activity of plasma Ch-E was inhibited more rapidly than that of brain Ach-E, whereas recovery of plasma Ch-E activity was more rapid than that of brain Ach-E. Recovery of brain Ach-E and plasma Ch-E was followed the model $Y=a+b(log_{10}X)$. Brain Ach-E activity and plasma Ch-E were inhibited 83% and 94%, respectively, at 60min after administered oral $LD_{50}$. Brain Ach-E and plasma Ch-E was inhibited in vitro by Terbufos