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:3.1.1.8 (cholinesterase)
12,691 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In order to identify and to characterize the antigens from Nippostrongylus brasiliensis which are involved in the in vitro blastogenesis of T cells from infected animals, we have established by crossed immunoelectrophoresis a two dimensional antigenic map of the adult worm homogenate. Polyclonal precipitating rabbit antiserum recognized 26 antigens including five enzymes in these homogenates. The antigenic enzymes, the precipitates of which are only stained by specific staining, are: aldolase, malic enzyme, acid phosphatase, peroxydase and cholinesterase. This antigenic map enable us to identify 26 antigens in adult worm homogenates and to compare them with those which will be contained in purification fractions from these homogenates or in homogenates from other parasites.
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PMID:Antigenic analyses of the adult worms of Nippostrongylus brasiliensis by crossed immunoelectrophoresis. 409 83

1. The action of beryllium on the following enzymes has been examined: alkaline phosphatase (Escherichia coli and kidney), acid phosphatase, phosphoprotein phosphatase, apyrase (potato), adenosine triphosphatase (liver nuclei, liver mitochondria, brain microsomes), glucose 6-phosphatase, polysaccharide phosphorylases a and b, phosphoglucomutase, hexokinase, phosphoglyceromutase, ribonuclease, A-esterase (rabbit serum), cholinesterase (horse serum), chymotrypsin. Alkaline phosphatase and phosphoglucomutase are inhibited by 1mum-beryllium sulphate whereas the other enzymes are largely unaffected by 1mm-beryllium sulphate. 2. Possible mechanisms for the inhibition of phosphoglucomutase and alkaline phosphatase are discussed.
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PMID:The inhibition of enzymes by beryllium. 428 87

Some enzymatic parameters of neuronal transmission as well as the occurrence and the properties or carboxylic ester hydrolases in the hippocampal region of the wistar rat are investigated by histochemical and comparable biochemical methods. The acetylcholinesterase-, the monoamine oxidase- and the GABA-transaminase reaction are found at fibre structures, the course of which is seen more or less clearly. The histochemical picture of these enzymes is very different in each hippocampal layer and mainly limited by the corresponding number of reacting fibres. The origin and attribution of the fibres to the afferent and efferent systems are discussed. The occurrence of the acetylcholinesterase, the monoamine oxidase and the GABA-transferase as well as of the biogenic amines and the GABA are hints for the existence of cholinergic as well as aminergic and GABA-ergic processes of transmission in the hippocampal region. In the hippocampal region, the cingular and the optic cortex carboxylic ester hydrolases acetylcholinesterase, unspecific cholinesterase and the A-, B- and C-esterase could be demonstrated. The acetylcholinesterase of the hippocampal region is for the most part firmly membrane-bound and exists at least in two multiple, formalin-sensitive forms which are histochemically located in fibre structures. The unspecific cholinesterase, localized in the hippocampal region within vessel and capillary walls, exists in an electrophoretic mobile, formalin-sensitive form. Nearly half of the enzymes is soluble. A preferred binding to definite cell organelles was not demonstrable. In the hippocampal region the 3 multiple forms of the A-esterase are formalin-instable lyoenzymes. Good solubility and high formalin-sensitivity are the reason, why A-esterases are not demonstrable with usually histochemical methods. In the hippo ampal region the B-esterase is tightly bound to n electrophoretic mobile formalin-sensitive form in the microsomal fraction. In the cytoplasm of the neurones the desmoenzyme appears more or less granular. The 3 multiple forms of the C-esterase are formalin-sensitive to a different degree. Good solubility and low formalin-sensitivity, compared to the A-esterases are responsible for the fact, that the C-esterases can be shown histochemically only after en-bloc-fixation. The reaction products are granular. The similar behaviour of C-esterase and acid phosphatase, stated by many tests, suggests the C-esterases of the B- and C-type results in the same reactivity of pyramidal and granular cells of the hippocampal region. Some small, very strongly reacting cells belong to other cell types (probably basket cells or polymorphic cells).
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PMID:[Histochemical and biochemical investigations of the hippocampus and neocortex of the Wistar rat. I. Carboxylic ester hydrolases, transmitter enzymes and transmitters of the normal animal (author's transl)]. 610 39

Acetylcholinesterase, glutamine synthetase, acid phosphatase and glutamate dehydrogenase activity in brain and cholinesterase activity in blood were investigated in mice exposed to 170 p.p.m. trichloroethylene (TCE) during 30 days. The neuronal enzymes remained unaffected which suggests that no general damage occurred to either the glia or the nerve cell populations. In accordance with this no effect was seen on acid phosphatase. In contrast, plasma butyrylcholinesterase increased twofold in exposed male mice while it was unaffected in females. Liver weight in males and females increased with a factor of 1.5 and 1.9, respectively.
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PMID:Neurotransmitter metabolizing enzymes and plasma butyrylcholinesterase in mice exposed to trichloroethylene. 612 57

Although zinc in traces is essential for the growth and well being of the animal, however a long-term treatment has been found equally toxic to the liver and kidney. Present report describes its effects on few key enzymes viz. alkaline phosphatase, acid phosphatase, 5-nucleotidase, lipase, glucose-6-phosphatase, and cholinesterase in the liver of rat, Rattus rattus albino. Histochemical observations have provided visual evidences on Zn-induced dysenzymia. The results have further been interpreted in terms of its effects on cellular organelle, levels of enzyme protein and microenvironment of the hepatic parenchyma.
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PMID:A note on dysenzymia in the liver of rats fed on zinc, an essential metal. 629 52

Exocrine acinar cells possess a unique system of basally located lysosomes. Cytochemically, these lysosomes do not contain acid phosphatase, but react positively for trimetaphosphatase (C Oliver: J Histochem Cytochem 28:78, 1980). The present study extends the morphological and cytochemical characterization of these lysosomes in pancreatic, parotid, and exorbital lacrimal acinar cells from Sprague-Dawley rats and National Institutes of Health Swiss mice. The basal lysosomes are highly pleomoric in nature, and frequently appear as a system of anastomosing tubules of varying width. The lysosomes have a close morphological relationship with both the rough endoplasmic reticulum and mitochondria. In addition to trimetaphosphatase activity, the lysosomes are reactive for aryl sulfatase B, thiolacetic acid esterase, and cholinesterase. Since the cholinesterase activity could not be inhibited by specific inhibitors, this activity is most likely due to the presence of nonspecific esterases. The results of this study confirm the lysosomal nature of the basal lysosomes and underscore the necessity of using multiple enzyme activities to identify and characterize lysosomes.
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PMID:Characterization of basal lysosomes in exocrine acinar cells. 630 50

Choline, acetylcholine and betaine used as a sole carbon source, effectuate in Ps. aeruginosa an acid phosphatase activity in addition to a cholinesterase activity. Induction of both enzyme activities was repressed by succinate or glucose. Cyclic AMP failed to relieve the repression produced by these compounds. Substrates not related to choline and used as a sole source of carbon, were inefficient to produce induction of both enzymes. The in-vitro action of choline, acetylcholine and betaine on Ps. aeruginosa acid phosphatase and cholinesterase has also been studied. To perform these studies periplasmic extracts obtained by EDTA-lysozyme treatment of the cells grown on choline or betaine as sole source of carbon, were used. Acid phosphatase activity was competitively inhibited by betaine, whereas the inhibition produced by choline and acetylcholine showed competitive and noncompetitive components. Cholinesterase activity was noncompetitively inhibited by betaine. At low acetylthiocholine concentration choline was an inhibitor of cholinesterase, whereas at high substrate concentration choline raised the hydrolysis rate of acetylthiocholine. These findings allow the conclusion that acid phosphatase and cholinesterase are specifically induced by choline and its metabolites derivatives. Kinetic results led us to postulate that acid phosphatase and cholinesterase contain a similar allosteric site. This site would either be of an anionic nature or show affinity to a methyl group or display both characteristics.
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PMID:Induction of acid phosphatase and cholinesterase activities in Ps. aeruginosa and their in-vitro control by choline, acetylcholine and betaine. 640 29

Different compounds derived from choline, and obtained by demethylation or by oxidation of the primary alcohol group with subsequent N-demethylation, were tested as inducer agents of acid phosphatase and cholinesterase in Ps. aeruginosa. It was found that betaine and dimethylglycine were the most effective inducers of both enzyme activities. These metabolites including choline itself, were not inducers of acid phosphatase and cholinesterase in other Gram-negative bacteria such as: Escherichia coli, Salmonella typhimurium, Shigella flexneri, Enterobacter liquefacciens and Proteus mirabilis. The acid phosphatase activities found in these bacteria were not inhibited in vitro by choline, betaine and phosphorylcholine. From these results it may be concluded that the acid phosphatase activity from Ps. aeruginosa is different from the same activity observed in the other bacteria. In addition, it is also shown that Ps. aeruginosa acid phosphatase and cholinesterase were inhibited by a number of compounds containing a positively charged amino group, with methyl or ethyl groups bound to it. These results seem to confirm that Ps. aeruginosa acid phosphatase and cholinesterase may contain a similar anionic site.
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PMID:Pseudomonas aeruginosa acid phosphatase and cholinesterase induced by choline and its metabolic derivatives may contain a similar anionic peripheral site. 643 82

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

Aiming at an improvement of the screening of toxic substances in biological materials and environment, the following biochemical indices were studied by means of the Tetrahymena pyriformis as a testing object: total protein, total lipids, glucose, lactate dehydrogenase (E.C.1.1.1.27.), gamma-glutamyl transferase (E.C.2.3.2.2.), aspartate aminotransferase (E.C.2.6.1.1.), alanine aminotransferase (E.C.2.6.1.2.), acetyl cholinesterase (E.C.3.1.1.7.), butyryl cholinesterase (E.C.3.1.1.8.), alkaline phosphatase (E.C.3.1.3.1.), acid phosphatase (E.C.3.1.3.2.) and alpha-amylase (E.C.3.2.1.1.). The study was conducted in the period of the population growth in an experimental medium with the minimum content of nutrients within the 96 hours of cultivation. It has been derived from the results that most of the enzymes are at the top of their activity in the early logarithmic stage of growth, i. e. in the period immediately following the log stage of population growth when the cells are getting ready for intensive division and growth; another peak activity period is the logarithmic growth stage--alkaline phosphatase and acid phosphatase are an exception with the culmination of activity in the stationary stage of population growth.
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PMID:[Selected biochemical indicators in the protozoan Tetrahymena pyriformis]. 644 37


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