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

Acetic acid was found to repress cholinesterase synthesis in the cells of Arthrobacter simplex var. cholinesterasus even at very low concentrations (0.1%). The repression is very stable. It is not eliminated by glucose or an organic acid of the Krebs cycle being added to the medium with acetic acid. The combination of acetic and butyric acids decreases the repression but does not eliminate it. The kinetics of cholinesterase synthesis was different in the cells grown on the medium with acetic acid and the cells cultivated on the medium with acetic acid and glucose, then washed and transferred to a fresh growth medium with glucose and acetylcholine as the sources of carbon.
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PMID:[Acetic acid, a catabolite repressor of cholinesterase synthesis by an Arthrobacter simplex culture]. 2 5

The anti-inflammatory activity of FL 70, a derivative of 2,5-dihydroxy-benzoic acid, was examined in a number of conventional experimental models. In addition, FL-70 was tested for its inhibitory action on enzymes. The results were as follows: 1. The induction of a local inflammatory reaction and the subsequent i.v. injection of trypan blue showed that FL 70 reduces the capillary permeability. 2, FL-70 significantly suppresses exudation in the formalin-induced peritonitis of the rat. 3. A slight inhibition of an edema in the footpad of the rat induced by formalin-dextran was not shown to be statistically significant. 4. Local swelling could be markedly inhibited in the turpentine-oil induced inflammatory reaction of the rabbit. 5. Exudation and formation of granulomatous tissue was inhibited in Selye's granuloma. 6. FL-70 markedly inhibited the local inflammatory reaction accompanying the cutaneous reaction in experimental vaccinia infection of the rabbit skin. The size of the infiltration after intracutaneous infection of the virus was not reduced. 7. FL-70 could not prevent the onset of clinical signs, if administered in experimental allergic encephalitis. 8. The activity of acid phosphatase was inhibited by FL-70. Alcaline phosphatase, cholinesterase, leucin aminopeptidase, glucose-6- phosphatase-dehydrogenase (G-6-PDH), trypsin and chymotrypsin were unaffe-ted. FL-70 inhibits the following, G-6-PDH activated reduction process: glucose-6-phosphate (see article).
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PMID:[Anti-inflammatory activity of a new quinoid polyradical (FL-70)]. 16 92

The purification of the pregnancy zone protein by means of immunoadsorbents is described. The pregnancy zone protein antibody was isolated from an absorbed rabbit antiserum and coupled with CNBr-activated sepharose. The pregnancy zone protein was isolated from pregnancy serum by the specific antibody cross-linked with sepharose. Contaminating serum proteins were eliminated by "inverse" immunoadsorption using antibodies against these proteins coupled with sepharose. An immunoelectrophoretically pure pregnancy zone protein was obtained. By means of a combination of immunoprecipitation and enzyme reaction in agar gel could be excluded that the pregnancy zone protein possesses activities of the following 11 enzymes: ceruloplasmin, leucine amino peptidase, alkaline phosphatase, carboxylic esterase, lactate dehydrogenase, malate dehydrogenase, glycerophosphate dehydrogenase, glucose-6-phosphat-dehydrogenase, cholinesterase, acetyl cholinesterase and oxytocinase.
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PMID:[Isolation of "pregnancy-zone" proteins using immuno absorbents and study of possible enzyme activities]. 17 12

Acetylcholine potentiated the glucose-induced insulin release from microdissected mouse islets of Langerhans but had no effect on basal insulin release. Significant potentiation was obtained with 0.1 micron acetylcholine in the presence of 10 micron eserine and with 1 micron or more acetylcholine in the absence of a choline esterase inhibitor. Carbamylcholine, too, potentiated insulin release. Potentiation was blocked by methylatropine, whereas methylatropine alone had no effect on insulin release. Acetylcholine or carbamylcholine (5-500 micron) had no obvious effect on cyclic GMP or cyclic AMP in the islets. In the presence of 11.1 mM D-glucose, the membrane potential of beta-cells oscillated slowly between a polarized silent state of -50 to -55 mV and a depolarized active state of -33 to -39 mV, at which a fast spike activity occurred. Acetylcholine made the potential stay at the plateau and induced a continuous spike activity pattern. Atropine inhibited the electrical effects of acetylcholine but not those of glucose alone. It is suggested that cholinergic potentiation of insulin release is mediated by changes of transmembrane ionic fluxes, probably without the intervention of cyclic GMP or cyclic AMP.
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PMID:Insulin release, cGMP, cAMP, and membrane potential in acetylcholine-stimulated islets. 21 36

The effects of pulsatile and nonpulsatile flow pattern on pancreas and liver blood flow were studied in nine dogs on cardiopulmonary bypass (CPB). Furthermore, plasma levels of glucose, insulin, glucagon, growth hormone, and cholinesterase were compared in 20 patients subjected to open heart surgery with either pulsatile or nonpulsatile perfusion. Impairment of liver and pancreas function was significantly greater at the end of CPB and 48 h afterwards with nonpulsatile flow as compared with the pulsatile flow pattern. A decrease of intestinal blood flow that was demonstrated in dogs subjected to nonpulsatile perfusion could at least in part be responsible for the difference in postoperative organ function observed in patients after CPB.
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PMID:[Comparative studies on pulsatile and continuous flow during extracorporeal circulation. Effects on liver function and endocrine pancreas secretion]. 45 49

Glutamate oxaloacetate transminase (GOT), glutamate dehydrogenase (GDH), sorbitol dehydrogenase (SDH), pseudo-cholinesterase (ChE) and various blood constituents were measured in the plasma of Japanese quail fed 1,1-di(p-chlorophenyl)-2-chloroethylene (DDMU) at low levels for periods ranging from 2 to 32 days. Previous work has shown that DDMU is a potent inducer of hepatic microsomal enzymes causing marked structural changes in the liver. A rapid increase in plasma GOT was observed within 4 days accompanied by an increase in relative liver weight. Plasma GDH and SDH increased to a maximum between 16 and 24 dyas which seems to be associated with hepatic cell proliferation. Plasma ChE showed a steady increase over the time course of DDMU administration. The level of plasma lipid was reduced after 4 days whereas the hepatic lipid content was substantially increased suggesting that the fatty liver condition may be caused by decreased release of triglyceride from the liver. Plasma glucose was reduced at 8 days but there was no evidence of a hyperglycaemic state. The changes noted after 2 days of DDMU diet were confirmed by measurements on birds 18 h after oral dosing the DDMU. The study demonstrates the value of plasma enzyme measurements for the early detection of toxic effects and indicates that DDMU administration leads to extrahepatic effects in addition to those previously described in the liver.
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PMID:The effects of 1,1-di(p-chlorophenyl)-2-chloroethylene on plasma enzymes and blood constituents in the Japanese quail. 46 32

The following parameters have been estimated in 15 red partridges (young adults of both sexes): 1. Biometry: relative weight of 10 organs (liver, kidneys, heart, brain, spleen, lungs, small gut, coecum, stomach, gizzard). 2. Hematology (mean +/- S.D.): Erythrocytes, 3.4 X 10(6) +/- 0.3 X 10(6) cells/mm3; packed cell volume 0.46 +/- 0.17; haemoglobin 103 +/- 27 g/l; mean red blood cell volume, 135.6 +/- 10.4 micrometer3; haemoglobin per red blood cell, 32.2 +/- 5,2 pg; haemoglobin concentration in red blood cells, 24.0 +/- 2.9 %; leukocytes, 36.9 X 10(3) +/- 7.8 X 10(3) cells/mm3; heterophilic, 32.3 +/- 8.3 %; basophilic, 5.3 +/- 1.5 %; eosinophilic, 1.4 +/- 1.5 %; lymphocytes, 56.1 +/- 7.3 %; monocytes, 4.6 +/- 1.4 %. 3. Blood biochemistry: Na +, 155 +/- 6 mEq/l; K +, 6.5 +/- 1.2 MEq/l; Cl--, 107 +/- 4 mEq/l; Pi, 53.3 +/- 14.4 mg/l; urea, 0.19 +/- 0.05 g/l; uric acid, 33.2 +/- mg/l; creatinin, 14.7 +/- 0.9 mg/l; glucose, 2.77 +/- 0.35 g/l; cholesterol, 1.38 +/- 0.36 g/l; total proteins, 44.1 +/- 5.9 g/l; albumin, 50.0 +/- 8.7 %; alpha globulins, 3.9 +/- 1.5 %; beta globulins, 7.5 +/- 2.2 %; gamma1 globulins, 31.5 +/- 5.6 %; gamma2 globulins 8.0 +/- 3.5 %. 4. Serum enzymology: Alkaline phosphatase, 8177 +/- 5078 u/l; SGOT, 356 +/- 138 u/l; SGTP 28.3 +/- 12.5 m/l; LDH, 955 +/- 570 m/l; GLD 12.6 +/- 12.4 u/l; CPD, 136 +/- 77 u/l; choline esterase, 2181 +/- 506 u/l. 5. Tissue enzymology: the 7 preceding enzymes have been estimated in 10 tissues listed in 1.
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PMID:[Biometry, hematology, plasma biochemistry and plasma and tissues enzymology of the red partridge (Alectoris rufa) (author's transl]. 60 40

The presence of active acetyl or butyryl groups and their acceptors in the growth medium was found to be necessary for the high rate of cholinesterase biosynthesis in the cells of Arthrobacter simplex var. cholinesterasus. The active acetyl and butyryl groups are formed upon hydrolysis of acetylcholine and butyrylcholine as well as in the course of glucose metabolism. The following acids were shown to be the acceptors of the acetyl and butyryl groups: butyric, succinic, fumaric, malic acids and, to a less extent, alpha-ketoglutaric acid. The active acetyl and butyryl groups are bound with the acceptors under the control of coenzyme A in the reactions of fatty acid synthesis and the tricarboxylic acid cycle. Presumably, CoA regulates cholinesterase synthesis. The high rate of CoA binding in metabolic reactions provides conditions for the intensive synthesis of cholinesterase; the deceleration of these reactions inhibits the biosynthesis of cholinesterase.
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PMID:[Effect of exogenous acetyl group acceptors on cholinesterase biosynthesis in Arthrobacter simplex cells]. 70 48

The effect of carbohydrates, aromatic alcohols, choline and acetylcholine on the biomass production and biosynthesis of choline esterase was studied with Arthrobacter simplex var. cholinesterasus. Fructose was found to be the best carbon source for the biomass accumulation and synthesis of choline esterase. Almost the same amount of the enzyme was produced on media with glucose and maltose as on the medium with fructose though the biomass yield was much lower. On the contrary, the biomass production was higher on media with acetylcholine and ethanol, but synthesis of the enzyme was inhibited. Choline was not assimilated by the culture. Differences in assimilation of glucose and fructose by the culture were found to depend on their concentration and the presence, or absence, of the inductor (acetylcholine) in the medium. Fructose was assimilated by the culture almost completely irrespective of its concentration and the presence of the inductor in the medium. Glucose was assimilated partly, best of all at a concentration of 0.5%. An increase of the concentration to 1% inhibited assimilation of glucose by the organism though had no effect on the biomass production and synthesis of the enzyme. The inductor stimulated assimilation of glucose by a factor of 1.5. Synthesis of choline esterase on the medium with acetylcholine at a concentration of 1% was increased more than twofold upon addition of glucose at a concentration of 0.1%. Biosynthesis of the enzyme rised with glucose concentration though accumulation of the biomass was inhibited. Inhibition of choline esterase synthesis on the medium with acetylcholine as a sole carbon source is due to a lack of energy and the absence of synthesis of carbon compounds which are acceptors of acetyl and methyl groups.
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PMID:[Effect of various carbon sources on cholinesterase formation by Arthrobacter simplex var. cholinesterasus]. 100 62

A description is given of an outbreak of equine infectious anaemia (E.I.A.) in Campania [at Naples and Aversa (Caserta)]; it was diagnosed by clinical, pathological and serological examinations (Coggins test). Using the serum of 45 horses with E.I.A. and 11 healthy horses (controls), numerous investigations were carried out on: enzymes, intrinsic coagulation factors, lipids and other substances. The results obtained were very interesting and show that in this disease there are significant increases in many enzymes (LDH, LAP, gamma-GT, CPK, PK and ALD) and copper. Insignificant increases were found in other enzymes (SDH, GLDH, MDH, ICDH, AIP, lysozyme, cholinesterase, GOT and GPT) and also intrinsic coagulation factors, lipid substances (total cholesterol, esterified cholesterol, triglycerides) and glucose. LDH-1-isoenzyme remains unchanged, whilst AcP decreases slightly.
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PMID:Biochemical studies on equine infectious anaemia. 101 May 2


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