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)

In this study, enzyme activities of the pancreatic appendages of the ductus hepatoPancreas (the so-called "pancreas") in Sepia officinalis L. have been demonstrated by light and electron micicroscopical methods: Malate dehydrogenase, monoamine oxidase, acid phosphatase, beta-glucuronidase, adenosine triphosphatase and carbonic anhydrase were shown by the former, and monoamine oxidase, catalase, glutamic oxalacetic transaminase, choline esterase (non-specific), alkaline phosphatase, acid phosphatase and carbonic anhydrase by the latter technique. The correlation between enzyme activity and distribution, and the presumed function of the two pancreatic epithelia is discussed.
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PMID:The localization of enzyme activities in the pancreatic appendages of Sepia officinalis L. (Cephalopoda). 15 95

A toxicological experiment on white male rats was carried out for one year. They received simultaneously per os nickel in doses 0.005 mg/kg and lead in doses 0.0025 mg/kg, equivalent respectively to the recommended by CMEA norms for nickel and hygienic norm for lead in drinking waters, as well as nickel and lead in doses 0.015 and 0.01 mg/kg, 0.015 and 0.1 mg/kg surpassing 3 and 4 times and 30 and 40 times the above mentioned norms or only nickel in doses 0.015 mg/kg, after which their effect on some enzyme indices was studied. Tests were made on: free sulfhydryl groups in blood serum, heart and liver; catalase activity of blood; cholinesterase activity and creatinphosphatase in blood serum; cytochromoxidase activity in liver and heart. It is established that in combined per os effect of nickel and lead in doses respectively 0.15 and 0.1 mg/kg and 0.015 and 0.01 mg/kg, as well as during independent effect of nickel with doses 0.015 mg/kg, occur disorders in the tissue breathing and oxyreduction processes. Nickel and lead in doses, equivalent to the hygienic norms, lead to no changes according to all studied indices.
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PMID:[The effect of chronic combined exposure to nickel and lead on the enzymatic indices in body uptake with the drinking water]. 136 56

The effect of mild doses of X-rays (three fractions, each of 100 R) on energy metabolism of the brain of starved rats has been investigated. It is inferred that X-radiation may cause serious detrimental changes of enzymes involved in glucose metabolism (glucose-6-phosphate dehydrogenase and fructose diphosphate aldolase) and in peroxidation (of catalase and lipid peroxidase), and of the acetylcholine activity which is determined by the cholinesterase level. Dynamics of changes in the protein and nucleic acid content of the brain has been studied. It has been shown that the level of 4-HIAA and 3M4HMA in the brain increases after irradiation of starved and normally fed rats.
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PMID:[The effect of low doses of x-rays on the biochemical processes in the brain and on urinary metabolites in fasted rats]. 188 96

The genetic structure of two Chukot Evens subpopulations (314 individuals) for electrophoretic protein systems and taste sensitivity to PTC was studied. 17 of the 39 loci were polymorphic (43.59%). The following systems were completely monomorphic: diaphorase NAD H (Dia); glucose-6-phosphate dehydrogenase (G-6-PD); glutamatoxalate transaminase (GOT); carbonic anhydrase (Ca-1); catalase (Ct), lactate dehydrogenase (loci LDH-A and LDH-B); leucine aminopeptidase (Lap); malate dehydrogenase (MDH); purine nucleoside phosphorylase (PNP); superoxide phosphorylase (PNP); superoxide dismutase (SOD); phosphoglucomutase-2 (PGM2); cholinesterase (locus E1); red cell esterase (4 loci); albumin (Alb); hemoglobin (Hb A and B); ceruloplasmin (Cp); and blood, gren, using the standard method. The following systems were polymorphic: red cell acid phosphatase (AcP); phosphoglucomutase-1 (PGM1); 6-phosphogluconate dehydrogenase (PGD); glutamatepyruvate transaminase (GPT); glyoxalase-1 (GLO-1); esterase (EsD); adenilatkinase (AK); alkaline phosphatase (Pp); cholinesterase (locus E2); haptoglobin (Hp); transferrin (Tf); group-specific component (Gc) and ABO, MN, Lewis, P blood groups and taste sensitivity to PTC. The following allele frequencies for polymorphic loci have been detected: AKI = 0.994; GLO = 1I = 0.082; GPT1 = 0.653; AcPA = 0.400; AcPB = 0.599; AcPC = 0.001; PGDA = 0.944; PGM1(1) = 0.906; EsD1 = 0.897; E2+ = 0.048; HpI = 0.394; GcI = 0,919; Tfc = 0.987; r(O) = 0.669; p(A) = 0.184; q(B) = 0.146; M = 0.711; Le = 0.411; P1+ = 0.521; t = 0.295. The genetic structure of Chukot Evens population is significantly nearer to that of the other ethnic groups of the North-East, in comparison with the genetic structure of Evenks of the Middle Siberia.
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PMID:[Genetic structure of the populations of native inhabitants in the northeastern USSR. V. The Chukot Evens]. 293 99

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 genetic structure of three Asiatic eskimos subpopulations (402 individuals), five coast chuckchies subpopulations (1793 individuals) and three reindeer chuckchies subpopulations (559 individuals) have been studied for 26 electrophoretic protein systems (33 loci). These are: adenilate-kinase (AK), diaphorase NAD X H (Dia), glyoxalase-1 (GLO-1), glucose-6-phosphate dehydrogenase (6GPT), glutamatpyruvate transaminase (GPT), glutamicoxalate transaminase (GOT), carbonic anhydrase-1 (Ca-1), catalase (Ct), acid phosphatase (AcP), lactate dehydrogenase (loci LDH-A and LDH-B), leucine aminopeptidase (Lap), malatedehydrogenase (MDH), purine nucleoside phosphorylase (PNP), superoxide dismutase (Sod), 6-phosphogluconate dehydrogenase (PGD), phosphoglucomutase (loci PGM1 and PGM2), cholinesterase (loci c1--c5), alkaline phosphatase (Pp), esterase D (EsD), red cell esterase (Est) - 4 loci, albumin (Alb), haptoglobin (Hp), hemoglobine (Hb A and B), group-specific component (Gc), transferrin (Tf), ceruloplasmin (Cp). In addition, AB0 and Rh system blood groups and phenyl thiocarbamide taste sensitivity (PTC) have been studied. 12 of 36 loci are polymorphic (33.33%), heterozygosity for all loci in eskimos, coastal and reindeer chuckchies being 0.118 +/- 0.005, 0.130 +/- 0.002 and 0.120 +/- 0.004, respectively. These estimates do not differ essentially from heterozygosity at these loci for mongoloid groups living further south. The test for interpopulation heterogeneity has permitted to estimate contribution of the loci to the differentiation of these populations. The least heterogeneity has been found at loci where gene frequency distribution is the most specific for these ethnic groups.
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PMID:[Genetic structure of the populations of native inhabitants in the northeastern USSR. III. Asiatic Eskimos and the coast and reindeer Chukchi]. 643 3

Acetylcholinesterase has an action in the central nervous system, independent of hydrolysis of acetylcholine. This study explored the possible interaction between the two molecules: the effects of acetylcholinesterase on the autoxidation of the catecholamine were tested, and, in turn, modification of the catalytic activity of the enzyme by products of dopamine oxidation were studied. Acetylcholinesterase selectively inhibited the speed of quinone production from dopamine as well as accumulation of hydrogen peroxide, whilst the rate of generation of superoxide was increased. Analysis of absorption spectra revealed the formation of a new product, which appeared after mixing acetylcholinesterase and dopamine in neutral pH. In all cases, butyrylcholinesterase was ineffective. Incubation of acetylcholinesterase in the presence of dopamine resulted in a significant decrease in the catalytic activity of the enzyme. The effects of application of preparations modifying autoxidation of dopamine (SOD, catalase, peroxidase) suggested that inactivation of the enzyme occurred as a result of the direct interaction of a quinone and/or semiquinone oxidation product with enzyme, as opposed to any effects of reactive oxygen species. Because acetylcholinesterase and dopamine are co-released from the neurons degenerating in Parkinson's disease, a direct chemical interaction between these two molecules could have significance both for the normal functioning of the substantia nigra and for related pathological states.
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PMID:A possible interaction between acetylcholinesterase and dopamine molecules during autoxidation of the amine. 774 5

The activities of glutamic-pyruvic transaminase (GPT) and catalase are increased by 42 to 283% in patients with neurodermatitis, eczema, and psoriasis, whereas the activities of glutamic-oxaloacetic transaminase, alkaline phosphatase, and cholinesterase are unchanged. In women with neurodermatitis and psoriasis the level of GPT is by 24-28% lower than in men. In psoriasis catalase activity in women is by 50% higher than in men. Hence, the activities of some enzymes in disease are related to patients' sex. Blood serum catalase measurements are diagnostically valuable in skin diseases.
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PMID:[Blood enzyme activities in men and women with certain diseases]. 775 54

Changes in selected enzyme parameters were followed in a one year-long toxicologic experiment on albino rat males given vanadium by mouth at either of two dosages: 0.005 mg/kg b.w., which is the equivalent of the regulated level for 1st category drinking water, or 0.01 mg/kg, i.e., twice the safety standard. The endpoints measured included: free sulfhydryl groups in blood serum, heart, and liver; cholinesterase and creatine kinase activities in blood serum; catalase activity in blood; and cytochrome oxidase activity in liver and heart. Chronic oral exposures to vanadium 0.01 mg/kg and, to a lesser extent, 0.005 mg/kg were observed to produce disturbances in redox processes and tissue respiration. The evidence from this study should be taken into consideration when regulating vanadium levels in drinking water from a hygiene standpoint.
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PMID:[An experimental study of the effect of vanadium on enzyme indices in chronic oral exposure]. 852 48

The mechanism of inactivation of cholinesterase (EC 3.1.1.8) by the Cu2+ -ascorbic acid (AsA) system was investigated. Incubation of the enzyme with the Cu2+ -AsA system under aerobic conditions resulted in an irreversible loss of enzyme activity. At low concentrations of Cu2+, the extent of inactivation showed the same dependence in accordance with the extent of oxidation of AsA. Saturation kinetics were observed with respect to the concentration of AsA. No change in the dissociation constant of the enzyme-AsA complex was observed at various concentrations of Cu2+. Catalase at a low concentration partially protected the enzyme from the inactivation, but did not affect the oxidation of AsA. In addition, catalase at a high concentration completely protected both the enzyme from inactivation and the AsA from oxidation. Both thiourea and thiocyanate completely protected the enzyme from the inactivation, while AsA was partially oxidized only in the initial phase. Our proposed mechanism for the inactivation of an enzyme by the Cu2+ -AsA system is as follows. A ternary complex involving the enzyme, Cu2+ and AsA is formed. This is followed by a redox reaction within the complex which generates a superoxide (.O2-) and hydrogen peroxide (H2O2). The H2O2 then reacts with .O2- in a Haber-Weiss reaction producing the hydroxyl radical (.OH). Another role of H2O2 is the conversion of the reduced Cu+ within the complex to Cu2+. Thus, repeated cycles of the redox reaction between the Cu2+ and AsA take place at the same locus, producing multiple .OH, which causes its complete inactivation.
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PMID:Inactivation of cholinesterase by ascorbic acid in the presence of cupric ions: a possible mechanism for the inactivation of an enzyme by the metal-catalyzed oxidation system. 884


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