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)

Activity of membrane-bound enzymes, passive penetration of ions in dose-dependent loading with cholesterol, effect of cholesterol high concentrations on the metabolic patterns in cytosol, viscosity of cell suspension were studied in erythrocytes. Passive cotransport of H+ and Cl- ions via erythrocyte membrane was increased with augmentation in viscosity of the cell suspension. After loading with cholesterol activity of acetylcholinesterase was increased while ATPase and glyceraldehyde-3-phosphate dehydrogenase activities were decreased. The alteration in the enzymatic activity occurred on those sides of the membranes, where these enzymes were localized. Activity of lactate dehydrogenase was decreased in cytoplasm of erythrocytes. The alterations detected may be important in development of ischemic syndrome in hyperlipoproteinemia.
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PMID:[Activity of membrane-bound enzymes, indices of metabolism in the cytoplasm and various physico-chemical properties of erythrocytes with increased cholesterol level]. 293 99

It is demonstrated by experiments with rabbits that the Ca2+-ATP-ase activity is stabilized when using combined anesthetics (diacetylcholine + halothane + N2O) as distinct from application of halothane. A decrease in the cholinesterase activity is less pronounced than under the halothane action but more than with the diacetylcholine application. A decrease in the Na+, K+-ATP-ase activity is observed with all types of anesthesia. A considerable inhibition of creatine kinase under the action of combined anesthesia and halothane and an increase of the lactate dehydrogenase activity under diacetylcholine application in mitochondria are shown. Reliable differences in the succinic dehydrogenase activity are not detected.
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PMID:[Effect of combined anesthetics on the activity of various myocardium enzymes]. 303 46

High-affinity choline uptake mechanisms are among the characteristics of cholinergic neurons such as the ciliary and choroid subpopulations in the ciliary ganglion (Barald and Berg, 1979). We have produced three monoclonal antibodies (Mabs), two of which were made to 8-day embryonic chick ciliary ganglion (CG) neurons (CG-1, CG-4) (Barald, 1982) and one of which was made to cultured mesencephalic neural crest (NC) cells (CG-14) removed from the embryo 31 hr after incubation. We have shown that all three Mabs label a common 75 kD antigen present on the cell surface of both CG neurons and NC cells (Barald, 1988). Here we report that the CG-1 and CG-4 antibodies, used in the same ratios in which they are synergistically cytotoxic for both the CG and NC cells (Barald, 1988), and Mab CG-14 alone, have specific effects on the high-affinity choline uptake mechanism (HACU) of CG neurons and isolated antigen-positive NC cells in the absence of complement. CG-1 and CG-4 in ratios of 8/1 (the same ratios that are used to kill the CG and the NC subpopulation), but neither singly, inhibit the HACU of CG neurons by 40% and that of isolated antigen-positive NC cells by 75%. However, CG-14 alone, at 1 microgram/ml, inhibits the HACU of both CG neurons and isolated NC cells by 95%. None of the antibodies had an effect on numbers of ouabain binding sites (a measure of the Na+/K+ ATPase) or cell surface acetylcholinesterase (AChE) of CG neurons or NC cells isolated by "no-flow" fluorescence cytometry with a Meridian Instruments ACAS470 cytometer. CG or NC cells grown in the presence of the antibodies without complement grow and remain healthy for many weeks. They exhibit no difference in morphology, protein content, lactate dehydrogenase activity (LDH), or division time from untreated sister cultures. Therefore, the antigen recognized by all three Mabs may be involved in a high-affinity choline uptake mechanism, a common characteristic of cholinergic neurons. The Mabs themselves may possibly label some element of the high-affinity transporter or a proximal membrane component. This implies that such a high-affinity uptake mechanism is present in the subpopulation of NC cells at early times in development. If these cells in fact are destined to contribute to the avian CG, these characteristics are present in the subpopulation before the NC cells take on a neuronal morphology.
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PMID:Antigen recognized by monoclonal antibodies to mesencephalic neural crest and to ciliary ganglion neurons is involved in the high affinity choline uptake mechanism in these cells. 321 16

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

Normal and preganglionically denervated cat superior cervical ganglia were sectioned and cultured for 24 or 48 hr, with or without preliminary inactivation of acetylcholinesterase, and in the presence or absence of 10(-5) M glycyl-L-glutamine. They were then homogenized, and the molecular forms of acetylcholinesterase were analyzed by sucrose gradient sedimentation. We observed an increased proportion of the globular monomeric G1 form, and to a lesser extent of the dimeric G2 and tetrameric membranous G4 forms, of acetylcholinesterase in the glycyl-L-glutamine-treated compared with the control cultures. There was only a small increase in the total acetylcholinesterase activity and no significant variation in the activity of the metabolic enzyme lactate dehydrogenase. It therefore seems likely that glycyl-L-glutamine, or the endogenous neurotrophic factor, maintains acetylcholinesterase in the preganglionically denervated ganglia in vivo by specifically increasing the biosynthesis of the monomeric G1 form, but not that of other proteins; these trophic factors do not seem to promote the polymerization of G1 into the more complex G2 and G4 forms.
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PMID:Effects of glycyl-L-glutamine in vitro on the molecular forms of acetylcholinesterase in the preganglionically denervated superior cervical ganglion of the cat. 342 56

The proposed system of continuous monitoring of enzyme activities is based primarily on the electrochemical behaviour of thiol compounds, and the experimental equipment is extremely simple. The determination of cholinesterase (EC 3.1.1.8) activity is described. The normal values obtained for men (73.9, s +/- 10.3 microkat/l) and for women (71.1, s +/- 10.2 microkat/l), lie within the usual range of analogous photometric methods. Systems for determination of the activities of alkaline phosphatase (EC 3.1.3.1) and adenosylhomocysteinase (EC 3.3.1.1) are described. The activity of aspartate aminotransferase (EC 2.6.1.1) is determined by a combination of enzyme reactions, in which CoA is released from acetyl-CoA. Analogous procedures are discussed for determinations of alanine aminotransferase (EC 2.6.1.2), lactate dehydrogenase (EC 1.1.1.27), lipase (EC 3.1.1.2), and phospholipase A2 (EC 3.1.1.4) activities, and for determination of substrates, e.g., acetate and carnitine. Possible determinations of an additional 199 enzyme activities and of some of substrates are suggested. By determining electrochemically active groups other than thiols this method becomes almost universally applicable.
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PMID:New system of continuous monitoring of enzyme activities and determination of some substrates. 344 Aug 58

We analyzed the activities of acetylcholinesterase and butyrylcholinesterase, and of the metabolic enzymes enolase and lactate dehydrogenase, in the superior cervical ganglion, ciliary ganglion, dorsal root ganglion, stellate ganglion, and caudate nucleus of the cat; we found that these tissues possess very different levels of enzymic activities. The proportions of the alpha alpha, alpha gamma, and gamma gamma enolase isozymes are also quite variable. We particularly studied the molecular forms of acetylcholinesterase and butyrylcholinesterase, in normal tissues and in preganglionically denervated SCG, in comparison with earlier histochemical findings. The results are consistent with the premise that the G1 (globular monomer) forms of both enzymes are located in the cytoplasm, the G4 (globular tetramer) forms are at the plasma membranes, and the A12 (collagen-tailed, asymmetric dodecamer) form of acetylcholinesterase is at synaptic sites.
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PMID:Distributions of molecular forms of acetylcholinesterase and butyrylcholinesterase in nervous tissue of the cat. 347 23

The intraperitoneal (IP) treatment of rats with diazinon (40 mg/kg) resulted in a variety of changes in the brain. Glycogen was depleted, but there was an increase in the activities of glycogen phosphorylase, phosphoglucomutase, hexokinase, lactate dehydrogenase, and fructose 1,6 diphosphatase. The activity of glucose-6-phosphatase was unaffected while that of cholinesterase was significantly reduced. Lactic acid content was increased, while that of pyruvate was not altered. Animals developed tremors and convulsions, which were maximal two hours after treatment. The induced changes may be compensatory mechanisms to provide extra energy to cerebral tissue as a result of the stimulatory effects in diazinon-treated animals.
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PMID:Cerebral glucose and glycogen metabolism in diazinon-treated animals. 350 78

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

1. A variety of biochemical measurements were taken periodically in captive northern bobwhite (Colinus virginianus L.), European starlings (Sturnus vulgaris L.), red-winged blackbirds (Agelaius phoeniceus L.) and common grackles (Quiscalus quiscula L.) to determine whether baseline values remain sufficiently stable throughout the year for general clinical use in the absence of concurrent control specimens. 2. Variables included whole blood hematocrit and hemoglobin, plasma lactate dehydrogenase, alpha-hydroxybutyrate dehydrogenase, aspartate aminotransferase, alanine aminotransferase, creatine kinase, butyrylcholinesterase, alkaline phosphatase, glucose, albumin, total protein, creatinine, urea nitrogen, uric acid, cholesterol, and triglycerides, and brain acetylcholinesterase. Butyryl- and acetylcholinesterase were included because of their specific uses in toxicology. 3. Significant seasonal differences were detected for each of the variables except brain acetylcholinesterase in at least one of the species. Significant species differences were detected during at least one season for all of the variables measured. 4. All species were maintained outdoors, but only northern bobwhites came into reproductive condition and showed sex-differences in the clinical variables during their normal breeding season. 5. It was concluded that reference values for the 18 clinical variables measured could be calculated from our data for adult specimens of the species studied, and that results for one species cannot be extrapolated with certainty to any other species. 6. Estimated normal bounds for each of the 18 variables measured by commonly used clinical procedures are presented for reproductively quiescent northern bobwhites, European starlings, red-winged blackbirds, and common grackles.
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PMID:Seasonal variation in diagnostic enzymes and biochemical constituents of captive northern bobwhites and passerines. 366 39


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