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)

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

The pseudocholinesterase levels and the nature of the enzyme as shown by the dibucaine number (D.N.) were estimated in 720 controls and 420 lepromatous leprosy patients, and 301 tuberculoid leprosy patients. There was no statistical difference in the esterase levels between leprosy patients and normal controls. But the distribution of D.N. was significantly different in the leprosy patients compared to the normal population studied. The D.N. below 40 indicates the samples with the atypical pseudocholinesterase--the presence of which is genetically determined. The distribution of samples with D.N. below 40 was significantly higher in the lepromatous leprosy patients compared to the normal population or tuberculoid leprosy patients. It is proposed that since there is a greater incidence of the atypical enzyme in lepromatous leprosy cases, the presence of this enzyme or the deficiency of the typical enzyme may make a person more susceptible to leprosy.
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PMID:Susceptibility to leprosy and serum atypical pseudocholinesterase. 98 94

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

1. The esterase isozymes of human tissues have been investigated using the technique of starch-gel electrophoresis. Conventional naphthyl-azo dye linked stains and new fluorogenic staining methods were used to detect the isozymes. 2. Multiple isozymes were identified in every tissue and they were characterized in terms of their electrophoretic mobility, tissue distribution, developmental changes in utero, substrate specificity, inhibition properties and molecular weight. On these criteria 13 sets of esterase isozymes were identified, in addition to the esterase isozymes due to cholinesterase and carbonic anhydrase. 3. The data suggest that the 13 sets of isozymes are determined by at least nine different structural gene loci. 4. No electrophoretic variants were identified in a limited population survey of post-mortem tissues from adults and foetuses, except for the previously described esterase D (ESD) phenotypes.
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PMID:A preliminary genetic interpretation of the esterase isozymes of human tissues. 118 Apr 83

The effect of hexafluorenium 0.3 mg/kg on the neuromuscular block of suxamethonium 0.1 mg/kg in a child with homozygote atypical plasma cholinesterase activity and in one of his normal brothers has been compared. In the normal child, hexafluorenium produced a marked potentiation of suxamethonium block, while partially antagonizing the block in the atypical homozygote child. In both situations, the hexafluorenium-suxamethonium block appeared to be antidepolarizing in nature as indicated by tetanic fade and post-tetanic facilitation. It is concluded that, in man, hexafluorenium can modify the action of suxamethonium by two different mechanisms. In patients with normal plasma cholinesterase activity, the anti-esterase effect predominates and results in marked potentiation of suxamethonium block, while in atypical homozygotes a direct antidepolarizing action at the neuromuscular junction may result in a diminished response.
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PMID:Hexafluorenium-suxamethonium interaction in patients with normal versus atypical cholinesterase. 120 Nov 67


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