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)

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

In a patient with paroxysmal nocturnal haemoglobinuria (PNH) enzymatic activities of erythrocytes and leucocytes were studied. Studies of autohaemolysis were also performed. The following erythrocytary enzymes were measured: Glucose-6-phosphate dehydrogenase (G-6-PD), pyruvate kinase (PK), glutathione reductase (GR), and acetylcholinesterase (AcChE). The following enzymes were measured in leucocytes: Adenosine deaminase, purine nucleoside phosphorylase, adenine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase and adenosine kinase. Normal activity of G-6-PD, GR and PK in erythrocytes was found. In leucocytes and lymphocytes activity of purine nucleoside phosphorylase was reduced. Auto-haemolysis in vitro was increased, which could not be compensated by addition of glucose or ATP.
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PMID:Erythrocyte and leucocyte enzymes in a case of paroxysmal nocturnal haemoglobinuria. 10 10

The alteration of two erythrocyte plasma membrane functions, acetylcholine hydrolysis and glucose exchange, by a series of structurally related small lipophilic compounds which exhibit antihemolytic behavior was studied. 2-Methyldimethylaminoazobenzene is a more potent inhibitor of acetylcholinesterase than the 3'-methyl analogue, while the unsubstituted compound fails to inhibit. Esterase inhibition by the 2-methyl compound is non-competitive and dependent on the anion composition of the assay buffer. The temperature dependence of acetylcholinesterase activity in the presence of the 2-methyl compound suggests that interaction with inhibitor is influenced by the state of lipids tightly bound to the enzyme. Glucose exchange is inhibited to the same extent by both methyl derivatives but not by the unsubstituted dye, and the temperature dependence in the presence of inhibitor is not grossly altered. The lack of correlation between inhibition of membrane function adn stabilization of erythrocytes against osmotic hemolysis is discussed.
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PMID:Differential perturbation of erythrocyte membrane-associated transport and enzyme activities by structurally related lipophilic compounds. 11 Mar 44

Red blood cell plasma membranes contain a number of enzymes: ATPases, anion transport protein, glyceraldehyde 3-phosphate dehydrogenase, protein kinases, adenylate cyclase, acetylcholinesterase. Most of them are tightly bound to the membrane and are present in small amounts. As a result, structural characterization of erythrocyte membrane enzymes has not yet been successful. Functional studies have, however, yielded a great deal of information. ATPases allow active transport of cations (calcium, sodium, potassium). Anion transport protein controls movements of chloride and phosphate ions, and of glucose and water. Among glycolytic enzymes: glyceraldehyde 3-phosphate dehydrogenase is partially bound to the membrane. Protein kinases catalyze the phosphorylation of several membrane proteins, one of which (spectrin) is involved in red blood cell mechanical properties. The physiological role of adenylate cyclase is unknown. Acetylcholinesterase is an ectoenzyme. Calcium-dependent ATPase, adenylate cyclase and phosphorylation of erythrocyte membrane proteins have been found abnormal in various conditions: hereditary spherocytosis, sickle-cell anemia, progressive muscular dystrophies, all of these disorders being associated with a decreased deformability of the erythrocyte.
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PMID:The enzymes of the red blood cell plasma membrane. 14 25

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

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 present study investigated the effect of insulin in vivo on the changes in the cooperativity of a membrane-bound enzyme. The allosteric inhibition by F- of the erythrocyte membrane acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) was studied during intravenous glucose tolerance tests in control and alloxan-induced diabetic rats. In the former group, the value of n decreased from 1.6 to 1.0 whereas it remained about 1.6 in the latter groups. Intravenous injection of insulin (30 U/kg) decreased the values of n in both groups. It is suggested that the in vivo insulin action on membrane cooperative enzymes could also take place in insulin target cells.
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PMID:Biomembrane cooperative enzymes. In vivo modulation of rat erythrocyte acetylcholinesterase by insulin in normal and diabetic conditions. 48 90

Distribution and activity of acetylcholinesterase (AChE) in the neurons of the central vagal nuclei at the level of the medulla oblongata were studied in intact and alloxan-diabetic adult male rats by Gomori's histochemical method. Peculiarities of intracellular distribution of the enzyme in the Nucl. dorsalis n. vagi (ND) and Nucl. ambiguus n. vagi (NA) of intact animals were demonstrated. Changes in the ratio of cholinergic neurons with moderate and strongly-positive AChE staining reactions were revealed in the ND of alloxan-diabetic rats. The dynamics of the changes attested to increased AChE activity of these neurons in response to insulin deficiency. The data obtained are additional evidence for the responsiveness of ND neurons to insulin deficiency, which was demonstrated earlier in alloxan-diabetic rats by karyometry (Akmayev and Rabkina, 1976 b). It is suggested that changes in the plasma glucose or insulin levels may be the stimulus that influences the activity of the ND cholinergic neurons. By means of this mechanism the central vagal nucleus at the medulla oblongata level may be implicated in the feedback control of insulin secretion.
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PMID:CNS--endocrine pancreas system. III. Further studies on the vagal responsiveness to insulin deficiency. 66 40


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