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)

Human erythrocyte ghosts were solubilized in a low ionic strength medium containing 1% Triton X-100 and subjected to electrophoresis in polyacrylamide gels containing Triton X-100. Five major bands were stained with Coomassie Blue, all except one band being heterogenous when re-electrophoresed in gels containing sodium dodecyl sulphate. It was possible to detect acetylcholinesterase, non-specific esterase, ATPase, alkaline phosphatase, 5'-nucleotidase, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase, and aldolase activities on the Triton-containing polyacrylamide gels. Two of the enzymes, ATPase and 5'-nucleotidase, showed substantial inhibition by Triton X-100 in quantitative studies. This appears to be a useful method for studying membrane enzymes in normal and pathological red cells.
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PMID:Polyacrylamide gel electrophoresis of human erythrocyte membrane enzymes solubilized with triton X-100. 89 Sep 65

The effect of enriched human plasma-cholinesterase preparation on the phase II block of succinylcholine chloride was studied in man during anesthesia and surgery. Intravenous administration of 8 esterase units/kg of plasma-cholinesterase did not show any discernible effect on the phase II block of succinylcholine chloride, while edorphonium 10 mg clearly antagonized the block. The finding of the present study suggests that the preparation may be ineffective for patients with a prolonged apnea following the administration of succinylcholine chloride.
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PMID:Effect of plasma-cholinesterase preparation on the phase II block of succinylcholine chloride in man. 91 67

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 26-years-old man injected himself intramuscularly with 3.75 gram of demeton methyl in an attempt to commit suicide. After 36 hours severe symptoms of poisoning developed with loss of consciousness and respiratory arrest. As symptomatic treatment failed to improve his condition has given injections of purified serum cholinesterase. This was followed by a rise in the cholin esterase levels and the increased activity was accompanied by a rapid and definite improvement in the clinical findings. The results clearly indicate the usefulness of this method of treatment. Transfusions of fresh blood to counteract the cholin esterase deficiency are inadvisable because of the risks of complications. Substitution therapy with serum cholinesterase must be accompanied by administration of large doses of atropine.
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PMID:[Treatment of alkyl phosphate poisoning with purified serum cholinesterase (author's transl)]. 96 94

The inhibitory effect of 3-diethylaminophenyl-N-methylcarbamate methiodide on rat brain acetylcholinesterase and horse plasma butyrylcholinesterase was studied in vitro. This quaternary carbamate is a more potent inhibitor of acetylcholinesterase than butyrylcholinesterase. Complete inhibition of acetylcholinesterase may be achieved without any inhibition of butyrylcholinesterase, i.e. that 3-diethylaminophenyl-N-methylcarbamate methiodide is a selective inhibitor of acetylcholinesterase. The inhibitory effect of different doses of this compound on plasma and liver butyrylcholinesterase and erythrocyte, brain, heart and diaphragm acetylcholinesterase of the rat was studied in vivo. With increasing doses of carbamate the inhibition of the enzymes in the plasma, erythrocytes, liver, heart, and diaphragm increased while the brain acetylcholinesterase was unaffected. The toxic action of carbamate studied was preferably due to acetylcholin esterase inhibition in the peripheral nervous system and this compound cannot penetrate the blood-brain barrier.
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PMID:Anticholinesterase action of 3-diethylaminophenyl-N-methyl-carbamate methiodide in vitro and in vivo. 97 52

In the diencephalon of two species of Gymnophiona (Amphibia) two neurosecretory nuclei were examined with histological (Alcian Blue, Aldehyde Fuchsin, Brookes Trichrome stain) and enzyme histochemical techniques (acid phosphatase, alpha-naphthyl acetate esterase, acetylcholinesterase (AChE)). In the preoptic nucleus two categories of secretory neurons were distinguished: large and medium sized neurons. The perikarya of both cell types contain very little neurosecretory material. The Alcian Blue method stained the medium sized neurons faintly but selectively. The tractus praeopticohypophyseus is marked by the presence of Herring bodies, which, however, are relatively scarce. The neurohypophysis, in contrast, contains large amounts of neurosecretory material. Both cell types of the preoptic nucleus are characterized by their very strong AChE and alpha-naphthylacetate esterase activity. The AChE also marks the tractus praeoptico-hypophyseus. In the large neurons acid phosphatase is present around the nucleus; in the medium sized neurons this enzyme is concentrated close to the origin of the axon. In the dorso-caudal hypothalamus a small group of neurons is stained with Alcian-Blue. These neurons, which also contain AChE, are located immediately under the ependyma which seems to be specialized in this region.
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PMID:Histological and histochemical observations on the neurosecretory cells in the diencephalon of Chthonerpeton indistinctum and Ichthyophis paucisulcus (Gymnophiona, Amphibia). 100 Jun 1

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

Hemolymph of the marine mollusc, Aplysia californica, contains four large particles: acetylcholinesterase, hemocyanin, a hemagglutinin, and a structure tentatively identified as erythrocurorin. We purified the acetylcholinesterase 20-fold by differential centrifugation and filtration through a column of 4% agarose. The freshly isolated esterase complex was found to have a sedimentation coefficient of 69, but the negatively stained enzyme lacked a definite structure in the electron microscope, and appeared as irregular aggregates of a 60 A subunit. The complex was unstable below pH 5 or during storage at 7 degrees. Under these conditions, enzymatic activity remained essentially unchanged. Treatment of the purified enzyme with trichloroacetic acid, organic solvents, and sodium dodecyl sulfate broke the complex down into two major subunits with molecular weights of about 70,000. Exposure of the enzyme to [3H]diisopropylfluorophosphate resulted in the labeling of one of these subunits. Although similar in specificity, the cholinesterase of the blood differed from the enzyme in Aplysia nervous tissue, which is associated with membrane. Treatment with sodium deoxycholate activated the membrane-associated enzyme but inhibited slightly that of the hemolymph; tyrocidine inhibited the hemolymph enzyme but not the enzyme of nervous tissue; and mild digestion with trypsin released the membrane-bound enzyme in an active, soluble form, but inactivated the enzyme of hemolymph. The other particulates of Aplysia hemolymph were partially characterized. Aplysia hemocyanin was similar in structure to other molluscan hemocyanins. When negatively stained, the unit particle appeared to be a disc with a diameter of 280 A and a width of 45 A. These discs were stacked to form long cylindrical arrays. The purified hemocyanin was found to contain 0.26% copper (dry weight). Using differential centrifugation and gel filtration we also obtained a 9-fold purification of Aplysia hemagglutinin. This particle was 120 A in diameter with a dark staining central core of 40 A consisting of 6 subunits. The particle tentatively identified as erythrocurorin appeared as a structure 200 A in diameter consisting of 5 V-shaped subunits.
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PMID:Isolation and characterization of acetylcholinesterase and other particulate proteins in the hemolymph of Aplysia californica. 111 86

Pseudocholinesterase (E.C. 3.1.1.8) activity was measured in plasma of whole blood, bank blood, and several commercially available blood protein solutions by means of a colorimetric assay technique at 25 degrees C, pH 7.7, and with butyrylthiocholine as substrate (Merckotest-R No. 3337). Activity of whole blood was 5.79 plus or minus 0.20 U x ml-1, of bank blood 4.53 plus or minus 0.27 U x ml-1, and of two human serum solutions (Biseko-R, Seretin-R) 3.05 plus or minus 0.13 and 3.04 plus or minus 0.22 U x ml-1, respectively (mean plus or minus S.E.M.). The other blood protein solutions contained no clinically significant esterase activity. Since transfusion of blood plasma has been suggested for treatment of cholinesterase deficiency and postoperative suxamethonium-induced muscle paralysis, an in-vitro attempt was carried out to correlate the amount of plasma necessary and the rise of pseudocholinesterase activity in the recipient's blood: A large amount of blood has to be transfused to yield a comparatively small increase in esterase activity. Thus, considering the potential hazards of blood transfusion, this treatment does not seem to be advisable.
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PMID:Pseudocholinesterase activity of human whole blood, bank blood, and blood protein solutions. 114 98

During an investigation of cousin marriages in Iceland, five brothers and sisters were found to be homozygous for the "silent" allele of plasma cholinesterase. Clinical information on two family members is presented and discussed, and the possibility of the presence of a "nearly silent" plasma esterase allele, in one of the family units investigated, is suggested.
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PMID:Serum esterases of Icelanders. I. A "silent" pseudocholinesterase gene in an Icelandic family. 114 10


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