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)

1. Disc electrophoresis was used to determine the esterase isoenzymes present in adults of the strigeoid trematode Alaria marcianae (La Rue, 1917). 2. Eight esterase bands were found with alpha-naphthyl acetate as the substrate and Fast Blue RR as the dye. 3. From results obtained with inhibitors, four different types of esterases were tentatively identified; cholinesterase (one band), ali-esterase or B-type (one band), arylesterase or A-type (2 bands) and acetylesterase or C-type (4 bands).
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PMID:Electrophoretic separation of esterases of Alaria marcianae (La Rue, 1917) (Trematoda). 31 43

A maximum of 22 bands comprising four esterase subgroups--acetylesterase, carboxylesterase, cholinesterase, and acetylcholinesterase--were detected following electrophoresis of lesser snow goose sera on polyacrylamide gels. A minimum of seven structural genes was surmised to be involved in the biosynthesis of these enzymes following physiochemical characterizations. The genetic variability of these loci was calculated to be 1.25% average heterozygosity, while 14.3% of the loci were polymorphic. These estimates of genetic variability were substantially lower than those reported for other vertebrate species. The low degree of genetic variability found in snow goose serum esterases coupled with the extensive protein multiplicity observed may possibly reflect an adaptive strategy based on "biochemical plasticity" rather than genic heterozygosity for this species. The nature of evolutionary forces acting upon multiple enzyme systems such as esterases is discussed. The concept of "conditional neutrality" is introduced and defined within this context.
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PMID:Isoenzyme status and genetic variability of serum esterases in the lesser snow goose, Anser caerulescens caerulescens. 92 42

A number of enzymes, presumably secreted by larvae of B. microplus under natural feeding conditions, have been investigated in the skin of previously unexposed calves 4 h after infestation at the attachment site. Carboxylic ester hydrolase activity was demonstrated in the dermis, immediately adjacent to the mouthparts, or in the attachment cone, depending on substrate and reaction pH. The carboxylic ester hydrolase acting on naphthol AS-D acetate (2-acetoxy-3-naphthoic-O-toluidide) at pH 7-1 was characteristically found in the dermis and not in the attachment cone. The use of specific inhibitors showed that this enzyme was primarily a B-esterase or carboxylesterase with possibly a small portion of C-esterase or acetylesterase. It is postulated that carboxylic ester hydrolase could contribute to the dilation observed in the subepidermal capillaries adjacent to the attachment sites of unexposed animals, through the formation of plasma kinins. Other enzymes demonstrated in the dermis, adjacent to the mouthparts, were triacylglycerol lipase, as an aggregated deposit, and small amounts of aminopeptidase (microsomal) and monophenol monooxygenase. Aminopeptidase (microsomal) was also demonstrated in the attachment cone or adjacent epidermis, according to the substrate used. No activity was found in the host tissue, in association with the attachment site, for either alkaline or acid phosphatase, acetylcholinesterase or cholinesterase, peroxidase or amine oxidase (flavin-containing), despite the intense histochemical reaction for the latter in the tissues of larvae.
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PMID:Boophilus microplus: characterization of enzymes introduced into the host. 102 62

Various 4-arylthiomethyl-2-oxo-1,3-dioxole derivatives IIIa-o were synthesized. Their hydrolysis rates by arylesterase (EC 3.1.1.2) and cholinesterase (EC 3.1.1.8) in human serum were evaluated. Some of them were not hydrolyzed by cholinesterase, but were hydrolyzed easily by arylesterase. Among the substrates, sodium 4-((5-methyl-2-oxo-1,3-dioxol-4-yl)methylthio)benzenesulfonate (IIIg) was selected for its substrate reactivity toward arylesterase and its good water solubility. In addition, neither aliesterase (EC 3.1.1.1), acetylesterase (EC 3.1.1.6) nor cholesterol esterase (EC 3.1.1.13) hydrolyzed the compound. IIIg is thus concluded to be a specific substrate for arylesterase. Our assay system for serum arylesterase using IIIg can be readily applied to an automatic analyzer in the diagnosis of liver cirrhosis.
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PMID:2-Oxo-1,3-dioxoles as specific substrates for measurement of arylesterase activity. 193 62

1. Esterases from tissues of the surgeonfish (Teleostei, Perciformes, Acanthuridae) are characterized electrophoretically and include several carboxylesterases, an acetylesterase, and an atypical pseudocholinesterase (pseudo-ChE). 2. The pseudo-ChE occurs in several isozymic forms including sialated and asialated slightly-anodal forms found principally in liver, and a larger, asialated asymmetric form that barely penetrates the 10% PAGE gel matrix found together with true AChE in epaxial muscle, brain, and eye. 3. Characterization of these three pseudo-ChE activities suggest that they are decidedly atypical in the intermediacy of their substrate and inhibitor specificities relative to classically-defined AChE and pseudo-ChE activities.
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PMID:An analysis of esterase activities from surgeonfish tissues yields evidence of an atypical pseudocholinesterase. 323 22

Ten different nonspecific esterases in both mouse (Mus musculus) and rat (Rattus norvegicus) testis were identified following the analysis of electrophoretic patterns using genetic, developmental, and biochemical criteria. None of the enzymes were unique to testis, although the pattern of activity was testis specific. The enzymes comprised, in each species, six carboxylesterases (EC 3.1.1.1), one arylesterase (EC 3.1.1.2), one acetylesterase (EC 3.1.1.6), and two butyrylesterases (tentative designation). Cholinesterase (EC 3.1.1.8) was not detected. Individual homology relationships were recognized between the two species for all of these activities, except three of the carboxylesterases; however, these were coded for by homologous gene clusters. Similarities between the two species extended to the developmental course of expression and the modulation of the pattern of activity by the testicular feminization (Tfm) mutation. We describe the effects of the sex reversal (Sxr) mutation in the mouse, as well as the distribution of individual activities between Leydig cells and seminiferous tubules. The results of earlier histochemical studies are interpreted in the light of the present investigation. The correspondence between mouse- and rat-testis esterases suggests that the results could serve as a basis for mammalian testis esterase systems in general.
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PMID:Nonspecific esterases of mammalian testis. Comparative studies on the mouse (Mus musculus) and rat (rattus norvegicus). 389 53

The multiplicity of soluble esterases in Raillietina tetragona, R. echinobothrida and R. cesticillus was studied by use of slab polyacrylamide gel electrophoresis. Five fractions of esterase activity were observed in R. tetragona, seven in R. echinobothrida and three in R. cesticillus. The various fractions of esterase activity of closely related species of Raillietina showed differential behaviour towards various chemicals. Based on the inhibitory effect of inhibitors p-CMB, EDTA, malathion, silver nitrate and eserine sulphate, the various esterases have been classified into arylesterase, carboxylesterase, acetylesterase and cholinesterase.
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PMID:A comparative study on esterases from three species of Raillietina. 654 Feb 80

A direct and continuous kinetic method for the fluorimetric assay of various hydrolases by using new, highly water-soluble substrates is described. The latter consist of esters of strongly fluorescent 1-hydroxypyren-3,6,8-trisulfonic acid trisodium salt with acetic, butyric, caprylic, and oleic acid. Km and vmax values are given for the hydrolytic activity of porcine liver carboxylic ester hydrolase, wheat germ lipase, candida cylindracea lipase, hog kidney acylase I, and bovine pancreas alpha-chymotrypsin, while others (acetylesterase, trypsin, and cholinesterase) were studied qualitatively. By proper choice of the substrate, a fair selectivity may be achieved. Detection limits as low as 1 microgram enzyme/ml are found in some cases. Advantages of these new substrates over existing ones are briefly discussed.
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PMID:Fluorimetric assay of hydrolases at longwave excitation and emission wavelengths with new substrates possessing unique water solubility. 684 35

We characterized the interaction of the prodrug dipivefrin hydrochloride (DPE) with esterase activity in the rabbit cornea. The esterases which were identified included: (1) cholinesterase, (2) acetylcholinesterase, (3) a mixture containing carboxylesterase, acetylesterase and arylesterase, and (4) a non-specific esterase. DPE suppressed all of their activities as well as that of the mixture containing carboxylesterase, acetylesterase and arylesterase, and a nonspecific esterase. However, its effect on cholinesterase was larger than on any of the other activities, suggesting that DPE is a better substrate for cholinesterase than for any of the other esterases. These measurements along with those of substrate-dependent inhibition of 14C-DPE hydrolysis indicated that the DPE-esterase interaction was competitive based on changes in the apparent Km values which were extracted from Lineweaver-Burk plots of esterase activity. The substrate for cholinesterase competed with DPE most strongly among substrates. These results seem to suggest that DPE is hydrolyzed by various corneal esterases, mainly cholinesterase.
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PMID:Characterization of esterases involved in the hydrolysis of dipivefrin hydrochloride. 844 67