Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.8 (cholinesterase)
 12,691 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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

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 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

Studied was the enzyme constellation, resp., activity of alkaline phosphatase (AP), glutamate-oxaloacetic transaminase (GOT), glutamate-pyruvate transaminase (GPT), aldolase (ALD), leucin-aminopeptidase (LAP), cholinesterase (CE), creatine phosphokinase (CPK), lactate dehydrogenase (LDH), ornithine carbamoyltransferase (OCT), and guanase (G) in a total of 360 clinically normal and lactating and dry cows of the Black-and-White and Simmental crossbreeds. Characteristic quantitative changes were found with GOT, GPT, ALD, LDH, and CPK both over the dry period and over the entire period of lactation. The activity of LAP, AP, OCT, and G was not influenced by the functional status of the animals. In the course of the analyses there were changes in the serum ALD, CE, and GOT, associated with the breed. The enzymes referred to were studied with a view to establishing their normal parameters needed for the practice as the base to demonstrate preclinical disturbances in individual organs and tissues of the cows during pregnancy and the puerperium.
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PMID:[Enzyme constellation in cows of the Simmental crossbreed and Black Pied breed during the dry period and lactation]. 367 21

Using fully mechanized analytical equipment, interference by haemolysis in the determination of 26 clinical chemical parameters was determined quantitatively by adding haemolysate to serum. Haemoglobin concentrations up to 6.6 g/l caused essentially no interference in the following determinations: albumin (immuno-nephelometric), alpha-amylase, calcium, chloride, cholesterol, cholinesterase, creatinine, iron, glucose, glutamate dehydrogenase, uric acid, urea, sodium, inorganic phosphate, total protein, transferrin and triglycerides. In the presence of haemoglobin, erroneously high values were found for: lactate dehydrogenase (haemoglobin higher than 0.2 g/l), aspartate aminotransferase, potassium and acid phosphate (haemoglobin higher than 1.5 g/l), creatine kinase (haemoglobin higher than 2.5 g/l) and alanine aminotransferase (haemoglobin higher than 3.4 g/l). Erroneously low values were found for bilirubin (haemoglobin higher than 0.8 g/l), alkaline phosphatase and albumin (by electrophoresis) (haemoglobin higher than 1.5 g/l) and gamma-glutamyltransferase (haemoglobin higher than 3.0 g/l).
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PMID:Haemolysis as an interference factor in clinical chemistry. 371 97

The authors presented the results of a study of enzymuria (cholinesterase, gamma-glutamine transferase, alkaline phosphatase, beta-galactosidase and lactate dehydrogenase with separate determination of N- and M-subunits) in 20 patients with a mixed form of glomerulonephritis (GN), 36 with the nephrotic form of GN and 13 patients with the hematuric form of GN. The clinical importance of the determination of enzymatic activity in the urine in GN of children lies in the recognition of the degree of damage of the glomerular filter as well as the nephrothelium. Basing on enzymuria pathophysiological syndromes found in various combinations in the above forms of GN were identified. Three degrees of damage of the permeability of the glomerular filter were defined for high molecular proteins. Differences in individual values of the activity of some enzymes gave rise to differential-diagnostic coefficients as well as differential-diagnostic tables which could be used for differential diagnosis between the GN mixed and nephrotic forms.
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PMID:[Clinical significance of enzymuria in glomerulonephritis in children]. 376 57


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