Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.1.7 (acetylcholinesterase)
28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activities of various enzymes present in brain homogenates were assayed biochemically (a) with no pretreatment, (b) following a standard microwave treatment in saline and (c) after a standard microwave treatment in formalin. All enzyme activity was lost after the microwave - formalin in treatment. Following microwave - saline treatment, the activities of alkaline phosphatase, 5'-nucleotidase, isocitrate and succinate dehydrogenases were reduced. In contrast, the activities of lactate and malate dehydrogenases were unchanged, and that of acetylcholinesterase apparently increased. Analogous outcomes were seen following attempted histochemical demonstrations of these enzymes. Thus satisfactory histochemical demonstration of all enzymes was achieved (except with alkaline phosphatase, lactate and malate dehydrogenases) following the microwave-saline pretreatment. Since acid phosphatase, catalase and peroxidase were also successfully demonstrated, it seems that microwave-saline pretreatments permit both retention of sufficient enzyme activity for histochemical demonstration to occur and retention of sufficient structural integrity for critical morphological investigations. Since the failure to stain the sites of lactate and malate dehydrogenases is not due to microwave inactivation of these enzymes, their demonstration may be possible by varying the staining procedures.
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PMID:Brain enzyme histochemistry following stabilization by microwave irradiation. 306 7

Changes of enzyme activity in the colostrum, milk, and serum samples of 14 mothers were followed. For the enzyme assay, the colostrum and the milk samples were diluted, 1:10 and 1:5, respectively. The activity of the following enzymes were measured: lactate dehydrogenase (LDH); gammaglutamyl transpeptidase (GGT); aspartate aminotransferase (ASAT); alanine aminotransferase (ALAT); cholinesterase; alkaline, and acid phosphatase. Milk, LDH, ASAT, and ALAT activities did not change during the first four days of lactation, yet were significantly higher than the corresponding activities of serum. The activity of GGT and alkaline and acid phosphatase in milk showed a marked decrease by day 4 postpartum; however, the GGT stayed much higher than that of serum, while the activity of the other two enzymes decreased to the level of the serum. By contrast, as compared to the colostrum, the cholinesterase activity in the breast milk showed a significant increase.
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PMID:Comparative analysis of enzyme activity in human colostrum, milk, and serum. 339 Aug 99

The effect of manganese pretreatment on acute toxicity of fenitrothion (FTH) was investigated in male rats by assessing the degree of enzymatic alterations. Oral administration of FTH (260 mg/kg) markedly inactivated cholinesterase (ChE) and carboxylesterase and elevated the activities of acid phosphatase, alanine aminotransferase and aspartate aminotransferase in different tissues 3 h after dosing. Pretreatment of rats with manganese (10 mg/kg, i.p.) 3 days prior to FTH application (260 mg/kg, p.o.) significantly enhanced these enzymatic changes. The results indicate that inhibition of esterases and elevation in other enzymes induced by manganese are likely to contribute to the increased enzymatic alterations observed following combined treatment.
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PMID:Studies on the interaction between manganese and fenitrothion in rats. 359 Feb 18

Adult Ascaridia galli and Heterakis gallinae obtained from the fowl (Gallus gallus) were treated in vitro with 10(-2) to 10(-5) M parbendazole and piperazine adipate for 10-60 min at 38 degrees C. Both the compounds at 10(-2) M caused mortality of A. galli and H. gallinae after a maximum of 30 min exposure. The effect of the drugs on the homogenates of the treated worm was investigated. Parbendazole (10(-2) M) inhibited malate oxidation by 68% in A. galli and 62% in H. gallinae. Piperazine adipate (10(-2) M) inhibited malate oxidation by 78% in both parasites. In A. galli oxaloacetate reduction was inhibited by 41 and 26% by 10(-2) M parbendazole and piperazine adipate, respectively; with H. gallinae this inhibition was found to be 39 and 55%, respectively. Aldolase activity in both the parasites was also inhibited by 10(-2) M parbendazole and piperazine adipate. Both compounds caused an inhibition of acid phosphomonoesterase activity, but the activities of lactate dehydrogenase and alkaline phosphomonoesterase were not affected significantly. Parbendazole (10(-2) M) had no significant effect on the cholinesterase activity of these parasites, but piperazine adipate (10(-2) M) caused an inhibition of 96% in A. galli and 93% in H. gallinae. The possible mode of action of the drugs is discussed.
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PMID:Effect of parbendazole and piperazine adipate on the activity of some enzymes of Ascaridia galli and Heterakis gallinae. 361 27

Benzoyl- and isopentenoyl phosphoric triamides (BPA and IPA) strongly inhibited urease activities from jack bean, soybean, watermelon seed, Proteus mirabilis, P. rettgeri, P. vulgaris, Mycobacterium smegmatis, and Ureaplasma urealyticum. Their I50 values (the final concentration causing 50% inhibition), independent of enzyme source, were 2-21 nM, which are about 1,000-fold lower than that of caprylohydroxamic acid, one of the most potent urease inhibitors. ATP-urea amidolyase activity was inhibited 50% by BPA at a higher concentration of 0.28 mM, but was not affected by IPA even at 1.3 mM. Thirteen kinds of hydrolases (trypsin, chymotrypsin, thermolysin, leucine aminopeptidase, papain, lipase, alpha-amylase, glucuronidase, asparaginase, arylsulfatase, alkaline phosphatase, acid phosphatase, and true cholinesterase), two oxidoreductases (catalase and alcohol dehydrogenase), three transferases (glutamic-oxaloacetic aminotransferase, gamma-glutamyl transpeptidase, and arylsulfotransferase) and two kinases (pyruvate kinase and creatine kinase) were not affected at all even at 1 mM BPA and IPA. Exceptionally, pseudo-cholinesterase from human serum was inhibited by BPA and IPA, whose I50 values were 70 nM and 10 muM, respectively, using acetylthiocholine as a substrate. These values increased to 0.55 muM and 54 muM, respectively, when acetylcholine was used as a substrate. These results show that N-acylphosphoric triamides potently and specifically inhibit urease activity at concentrations of nM order.
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PMID:Specific inhibition of urease by N-acylphosphoric triamides. 384 42

The effect of dichlorvos and metathion was studied as exerted on acetylcholinesterase activity in the protozoan Tetrahymena pyriformis. In dichlorvos, the highest enzyme activity inhibition was obtained after 30 minutes. A 50% inhibition of the enzyme activity was recorded at the dose of 1.22 mg per litre. As to metathion, the highest enzyme activity inhibition was obtained after 60 minutes. A 50% inhibition of the enzyme activity was recorded at the dose of 879.2 ng per litre. One hour after exposure to this dose, almost 75% inhibition of the activity of the enzyme was recorded. The determination of acetylcholinesterase activity increases the sensitivity of the bioassay for organophosphates with the use of the Tetrahymena pyriformis protozoan. Dichlorvos was studied for its action at supratoxic doses (50.0, 100.0 and 150.0 mg per litre) and it was found that lactate dehydrogenase activity was almost completely suppressed; the inhibition of alanine aminotransferase was pronounced. A weaker activity inhibition was recorded in aspartate aminotransferase, alkaline and acid phosphatase; the activity of alpha-amylase increased. No dependence on dosage was demonstrated.
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PMID:[The effect of dichlorvos and metathion on selected enzymes of the amoeba Tetrahymena pyriformis]. 392 68

Blood samples taken from domestic or wild ruminant animals typically require transportation to an analytical laboratory. Depending on circumstances, several hours or even a few days may pass between sampling and analysis. Several diagnostic plasma enzymes were measured in bovine blood samples immediately after sampling and after storage under a variety of conditions. Conditions studied included storing whole heparinized blood at 20 C for 6 hours, storage at 4 C for 3 and 5 days, and freezing freshly prepared plasma once and 4 times before analysis. For studies of erythrocyte enzymes, fresh erythrocytes were compared with erythrocytes frozen once, frozen 4 times, and prepared from whole blood stored for one week at 4 C. None of these conditions deteriorated erythrocyte acetylcholinesterase. The serum pseudoacetylcholinesterase and lactate dehydrogenase were not affected by any storage condition used. By contrast, acid phosphatase was significantly decreased by all storage conditions used. Ornithine carbamoyltransferase, alkaline phosphatase, aspartate aminotransferase, and alanine aminotransferase were stable under some of the storage conditions tested.
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PMID:Storage stability of some bovine plasma enzymes. 392 97

The changes in brain acetylcholinesterase (AChE), acid phosphatase (APase), and 2',3'-cyclic nucleotide-3'-phosphohydrolase (CNP), and plasma butyrylcholinesterase (BuChE) activities were investigated in hens treated with a single, dermal dose (100-1000 mg/kg) of S,S,S-tri-n-butyl phosphorotrithioate (DEF). Three control groups consisted of hens left untreated, given a single, dermal dose of 500 mg/kg tri-o-cresyl phosphate (TOCP, positive control for organophophorous compound-induced delayed neurotoxicity), or 10 mg/kg O,O-diethyl O-4-nitrophenyl phosphorothioate (parathion, negative control). Brain AChE activity, determined 28 days after application, was significantly inhibited in hens given 500-1,000 mg/kg DEF and in TOCP- and parathion-treated hens. In contrast, brain APase and CNP activities were significantly higher in all treatments as compared with those of the untreated hens. Parathion, however, caused the least increase in these enzymatic activities as compared to DEF or TOCP. A single, dermal dose of DEF or TOCP also caused an initial decrease in plasma BuChE activity with maximum depression of enzymatic activity observed 1 to 7 days after administration. This decrease was dose dependent and the enzymatic activity showed partial recovery with time. Hens treated with single, dermal doses of DEF, ranging from 250 to 1000 mg/kg, developed ataxia which progressed to paralysis in some hens. Histopathologic examination revealed axon and myelin degeneration of the spinal cord and peripheral nerves of some hens. The severity and frequency of the neuropathologic lesions were dose dependent. Neurologic dysfunctions and neuropathologic lesions seen in DEF-treated hens were similar to those exhibited in TOCP-treated hens. While parathion produced acute cholinergic effects, it did not cause delayed neurotoxicity. The changes in brain and plasma enzymes are discussed in relation to their role in the pathogenesis of DEF-induced delayed neurotoxicity.
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PMID:Brain acetylcholinesterase, acid phosphatase, and 2',3'-cyclic nucleotide-3'-phosphohydrolase and plasma butyrylcholinesterase activities in hens treated with a single dermal neurotoxic dose of S,S,S-tri-n-butyl phosphorotrithioate. 395 29

Inhibition in acetylcholinesterase and alkaline phosphatase activities with an elevation in acid phosphatase activity were recorded in a freshwater prawn, Macrobrachium lamarrei (H. Milne Edwards) after sublethal dichlorvos exposure under static conditions. The possible role of these enzymes in the physiology of prawns and the probable mechanism of these changes in relation to dichlorvos intoxication are briefly discussed.
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PMID:Dichlorvos intoxication in a freshwater prawn, Macrobrachium lamarrei (H. Milne Edwards). 400 39

Exposure of freshwater prawn (Macrobrachium lamarrei (H. Milne Edwards) to a lethal dose (96-hr LC50;0.78 mg/l) of dichlorvos for 24, 48, 72, and 96 hr induced inhibition in acetylcholinesterase and alkaline phosphatase activities and enhanced acid phosphatase activity. Hepatic glycogen values were depleted while the blood glucose level was increased up to 72 hr of exposure. After 96 hr of dichlorvos exposure hypoglycemia was recorded. The possible role of these changes in the dichlorvos intoxication is discussed.
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PMID:Nature of dichlorvos intoxication in a freshwater prawn, Macrobrachium lamarrei (H. Milne Edwards). 401 89


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