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)

Activities of 12 enzymes (amylase, lipase, cholinesterase, nonspecific carboxyl esterase, lactate dehydrogenase (LDH), alkaline phosphatase, glutamate-oxalacetate transaminase (GOT), glutamate-pyruvate transaminase (GPT), gamma-glutamyl transferase (gamma-GT), leucine aminopeptidase (LAP), malate dehydrogenase (MDH) and peroxidase) were determined in the perienteric fluid and homogenate of Ascaris suum. With the exception of amylase, all activities were higher in the homogenate than in the perienteric fluid. The enzyme activities in the perienteric fluid were then compared with those in the human serum. Comparable activities were demonstrated for LDH, LAP, lipase and alkaline phosphatase, markedly higher activities in perienteric fluid were demonstrated for MDH, GOT, GPT and amylase, and much lower for cholinesterase. No gamma-GT activity was detected in the perienteric fluid.
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PMID:Activities of some enzymes in the perienteric fluid of Ascaris suum. 619 63

We describe a new method for measuring the in vitro rate of hydrolysis of the muscle relaxant succinylcholine. This substrate is hydrolyzed by plasma cholinesterase (EC 3.1.1.8). The resulting choline is determined by measuring the hydrogen peroxide formed on its oxidation by choline oxidase (EC 1.1.3.17). This is done by use of phenol and aminoantipyrine coupled to peroxidase, and yields an intense chromophore, Amax 500 nm. The assay requires 0.1 mL of plasma, and is precise and specific. The CV was 2.7% within run, 7.3% between run. For the usual (U variant) enzyme the Km is 53 mumol/L. Enzyme activity is removed by anticholinesterase antiserum, and is inhibited by dibucaine with a Ki of 2 mumol/L. Ten samples can be assayed in duplicate in an hour. This method is suited to routine use in any laboratory that has a simple spectrophotometer. The mean activity in 11 individuals with the cholinesterase phenotype UU was 105 U/L, for seven UA heterozygotes 61 U/L, and for three AA homozygotes 4 U/L. To the extent allowed by extrapolation from in vitro to in vivo results, this method should increase diagnostic accuracy and may directly predict duration of succinylcholine-induced apnea.
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PMID:A new succinylcholine-based assay of plasma cholinesterase. 636 11

We report the evaluation of a new commercially available assay system for the determination of serum pseudocholinesterase (EC 3.1.1.8) catalytic activity, and its application to a kinetic analyser. The assay is based on the colorimetric method of Okabe et al. (Clin. Chim. Acta 80, 87-94 (1977]: choline, liberated from benzoylcholine by pseudocholinesterase, is oxidized by choline-oxidase (EC 1.1.3.17) to betaine with the simultaneous production of hydrogen peroxide, which oxidatively couples with 4-aminoantipyrine and phenol in the presence of peroxidase to yield a coloured compound with maximal absorbance at 500 nm. The procedure not only has the advantage of being continuous, colorimetric and totally enzymatic but also appears to be precise (between-day analysis gives coefficient of variation between 3.5 and 5.6%) and accurate; the results obtained from normal and pathological sera show excellent correlation with those obtained by the alternative procedures employing propionylthiocholine, acetylthiocholine and butyrylthiocholine as substrates.
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PMID:Evaluation of a new continuous colorimetric method for determination of serum pseudocholinesterase catalytic activity and its application to a centrifugal fast analyser. 651 97

To determine the pathomechanism of the condition of CF 1 mutant mice which present paralytic club feet, anatomicohistological analysis (conventional histological staining, silver impregnation, cholinesterase staining, and retrograde tracer technique of horseradish peroxidase (HRP)) were carried out. CF 1 homozygotic mutant mice lacked the common peroneal nerve, while tibial nerve is larger than that of normal mice when they were compared at the similar levels of the posterior limbs. Anterior and lateral crural muscles of the homozygotic mutant mice except for peroneus longus and brevis muscles showed large group muscle atrophy. HRP study indicated that the number of HRP labeled cells after injection of HRP into the anterior and lateral crural muscles decreased remarkably in number in the homozygotic mutant mice, comparing with that of the normal mice.
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PMID:A morphological analysis of a new mutant mice with paralytic club feet, peroneal muscular atrophy (pma). 667 99

The developmental changes in the distribution of acetylcholine receptors (AChRs) and cholinesterase (ChE) were investigated in the posterior latissimus dorsi (PLD) muscle of chick embryos by double staining with rhodamine-labeled erabutoxin b (TMR-Eb) for AChRs and Karnovsky's method for ChE. During the development, the TMR-Eb and ChE positive areas changed in their shapes and sizes. In early stages, the TMR-Eb positive areas appeared as fine fluorescent dots of about 0.3 micrometer in diameter or small aggregates of such dots. These areas then became enlarged and exhibited the following sequential changes in their configuration: spindle-, round-, ring-, C- and finally tree-shaped. The transformation in the configuration of the areas appeared to be caused by the changes of the fluorescent dots in their number and distribution. Simultaneous staining with ChE revealed that at early stages the TMR-Eb positive areas were not stained with ChE, but then they were stained later. The ChE deposits usually accumulated at the borders of the TMR-Eb positive areas and thereby outlined them. Electron microscopy using horseradish peroxidase-labeled erabutoxin b revealed that the fluorescent dots represent the discrete regions of high AChR concentration at the muscle membrane.
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PMID:Acetylcholine receptors and cholinesterase in developing chick skeletal muscle fibers. 713 47

A choline oxidase-peroxidase coupled enzyme procedures is proposed for the determination of cholinesterase activity in human serum. This system is not only kinetic and colorimetric but is also relatively quick and simple to perform. The initial comparisons suggest that this method correlates well with a commonly used propionylthiocholine-dinitrobis-(nitro-benzoic acid) technique. Large amounts of bilirubin in the sample appear to have only minor deleterious effects on the assay. Since there are only two reagents that may be premixed, the procedure appears to be amenable to automation. The use of a mixture of sodium 2-hydroxy-3,5-dichlorobenzenesulfonate and 4-aminoantipyrene in the peroxidase catalyzed indicator reaction provides for a marked increase in sensitivity over previously reported 4-aminoantipyrene-phenol systems. This augmented sensitivity provides for a relatively large reagent to sample ratio. In addition, the reagents lend themselves toward lyophilization or "dry-fill".
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PMID:A procedure for the kinetic colorimetric determination of serum cholinesterase activity. 713 38

The cytoarchitecture of the motoneuron pool of the male rat was studied at the lumbo-sacral transition area, particularly in L6. In the latter segment a dorso-medial (DM), ventral (V), dorso-lateral (DL), and retrodorso-lateral group (RDL) could be defined. The DL group was associated with a prominent longitudinal dendrite bundle and the CM group with smaller transverse bundles. Moreover, close soma-somatic apposition was found between neurons in these columns. Because L6 gives rise to n. pudendus and contributes to n. ischiadicus, horseradish peroxidase (HRP) was applied to the cut n. ischiadicus and in other experiments injected into the pelvic muscles. Neurons in RDL were labeled following exposure of n. ischiadicus to HRP. Injections in m. levator ani resulted in labeled neurons in the V group, mainly below L6. Injections in m. sphincter urethrae resulted in labeled neurons in the DL group as well as neurons immediately cranial to this column. Musculus ischiocavernosus injections resulted in transport of HRP to neurons in the DL group, primarily in its medial part, and to more cranially located neurons. In addition, some neurons in the V group in L6 were labeled. Following injections in m. bulbocavernosus and m. sphincter ani, labeled neurons were found primarily in the DM group, and to a lesser extent in the V group. Histochemical investigations with staining methods for the localization of acetyl cholinesterase (AChE) and heavy metals (the Timm method) demonstrated that part of the neuropil of DL and of DM were different from the rest of the motoneuron neuropil. In the DL group the area with the diverging staining patterns corresponded to the region of the dendrite bundle. The experimental data indicated and the ultrastructural studies demonstrated that the histochemical differences could be correlated with differences in the composition of the populations of boutons. The comparison of the cytoarchitectural and histochemical data with the results obtained by the aid of the retrograde HRP tracing technique established that mm. sphincter urethrae, ischiocavernosus, bulbocavernosus, and sphincter ani were each innervated by two populations of neurons that were situated in separate areas which had different histochemical properties, and which thus probably have different compositions of their afferent inputs. The duality in the motoneuron pool that innervates the pelvic mucscle might be a reflection of the dual influence on these muscles. As all other striated muscles the pelvic muscles are under voluntary control. However, they are also tightly linked to the function of the pelvic viscera and thus under influence of the autonomic nervous system.
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PMID:Organization of the motoneurons innervating the pelvic muscles of the male rat. 741 45

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

Plasma myeloperoxidase levels in patients with cirrhosis were compared with those in patients with chronic hepatitis and healthy controls by means of a specific radioimmunoassay for myeloperoxidase. The mean concentration of plasma myeloperoxidase in cirrhotic patients (309.1 +/- 17.2 ng/ml, n = 41) was markedly higher than that in chronic hepatitis patients (222.6 +/- 17.2 ng/ml, n = 21) (p < 0.01) and normal controls (219.5 +/- 5.7 ng/ml, n = 50) (p < 0.01). Plasma myeloperoxidase showed good negative correlations with neutrocyte count (r = -0.32, p < 0.01), thrombocyte count (r = -0.40, p < 0.01), red blood cell count (r = -0.32, p < 0.01), serum albumin (r = -0.35, p < 0.01), and cholinesterase (r = -0.32, p < 0.02) and positive correlations with serum alkaline phosphatase (r = 0.49; p < 0.01) and lactate dehydrogenase (r = 0.31, p < 0.01) in patients with cirrhosis or chronic hepatitis. Among lactate dehydrogenase isozymes, a good positive correlation was seen between plasma myeloperoxidase and lactate dehydrogenase-2 (r = 0.40, p < 0.01) and lactate dehydrogenase-1 (r = 0.03, p < 0.02). Plasma myeloperoxidase was significantly higher in the cirrhotic and chronic hepatitis patients with splenomegaly (341.1 +/- 19.4 ng/ml, n = 31) than in those without splenomegaly (217.4 +/- 12.2 ng/ml, n = 29) (p < 0.01). We also examined the difference between plasma levels of myeloperoxidase in the portal and peripheral blood.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:High plasma concentration of myeloperoxidase in cirrhosis: a possible marker of hypersplenism. 824 62

2-Naphthyl acetate acts as a pro-enhancer of the luminol-H2O2-horseradish peroxidase reaction. Cholinesterase hydrolyses the bound acetyl group and produces 2-naphthol, and this compound is an enhancer of the chemiluminescent reaction. We studied the kinetics of chemiluminescent emission and the influence of 2-naphthyl acetate and cholinesterase enzyme concentrations. The cholinesterase concentration versus chemiluminescence intensity maximum was linear for cholinesterase between 0 and 181 microU/mL, with a detection limit of 8 microU/mL and a relative standard deviation of 9.5% (n = 3), for a sample containing 90.67 microU/mL of cholinesterase.
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PMID:Assay of cholinesterase using a pro-enhancer of the luminol-H2O2-horseradish peroxidase reaction. 853 10


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