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)

Activity of pseudocholinesterase (acylcholine-acyl-hydrolase) elevated up to four times has been detected in sera of members of two German families. The catalytic concentrations of the pseudocholinesterase of the afflicted members of both families (male and female) varied between 4800 U/l and 10 200 U/o (acetylthiocholine iodide substrate). The pseudocholinesterase of the propositi exhibits isoenzyme separation patterns in polyacrylamide electrophoresis as well as in electrofocussing which are different from those of pseudocholinesterase from normal persons. No differences could be seen as regards the Km of substrates or the inhibition by dibucaine, fluoride or succinyldiocholine.
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PMID:A rare genetically determined variant of psuedocholinesterase in two German families with high plasma enzyme activity. 48 19

No hydrolysis of etomidate in plasma in vitro was detected in samples from man, horse, cow, sheep, guinea pig or white rabbit. Brown rabbits showed a moderate degree of hydrolysis and it was marked in plasma from Wistar rats. In this species, a single enzyme, an alliesterase, participated in the hydrolysis in plasma. Etomidate did not interfere with the hydrolysis of procaine by plasma pseudocholinesterase in man.
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PMID:Etomidate and plasma esterase activity in man and experimental animals. 49 34

Four-hundred and ninety individuals belonging to the Vysya caste from Andhra Pradesh were screened for pseudocholinesterase variants at the E1 and E2 locus. A high incidence of the silent allele (gene frequency=0.1112) was recorded with homozygotes exceeding 2% of the population. Dibucaine- and fluoride-resistant alleles were found in a heterozygous form with the usual alleles in four individuals each. No C5+ variant at the E2 locus was found.
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PMID:High incidence of the silent allele at cholinesterase locus I in Vysyas of Andhra Pradesh (S. India). 52 75

The frequency of the serum atypical pseudochloinesterase variant was significantly higher (p less than 0.005) in a group of 115 lepromatous leprosy patients than in a comparison group of 133 healthy individuals. This finding corroborates the results obtained in the group of patients from India, and supports the contention that the serum atypical pseudocholinesterase is one of the possible genetic factors involved in susceptibility to leprosy.
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PMID:Serum atypical pseudocholinesterase and leprosy. 52 4

The results of measurements made in two cases of tetanus suggest that the level of tetanus antibody in the blood cannot be used as a diagnostic test for the disease. The investigation also indicated that an attack of tetanus does not result in a rise in tetanus antitoxin antibody levels. This confirms the opinion that tetanus is not an immunising disease. In the cases described, the pseudocholinesterase level was not of diagnostic value.
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PMID:The immunology of tetanus. 53 22

No difference in the distribution of serum pseudocholinesterase variants could be found in lepromatous leprosy patients as compared with controls. The variety of reported relationships of pseudocholinesterase variants in leprosy suggests that only in some populations is a locus regulating pseudocholinesterase genetically linked to a hypothetical locus regulating susceptibility to leprosy.
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PMID:Serum pseudocholinesterase variants in Mexican-born patients with lepromatous leprosy. 56 47

Pseudocholinesterase activity was investigated in three groups of unselected patients. A slight rise of the enzyme was found during surgery under local anesthesia with lidocaine. In general anesthesia with thiopentone and halothane, the pseudocholinesterase activity diminished. The inhibition was more pronounced when pancuronium had been injected. From these data one may conclude that pancuronium must be carefully given in patients with low level of pseudocholinesterase when other drugs inhibiting the enzyme activity, like succinylcholine, procaine and propanidid, are used.
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PMID:Pseudocholinesterase changes in anesthesia using pancuronium. 61 15

Using exogenous substrate for its assay, lecithin:cholesterol acyltransferase (LCAT) was found to be decreased in liver disease and higher than normal in endogenous hypertriglyceridemia. LCAT activity was positively correlated with serum cholesterol and triglyceride. However in the six patients with excessive hypertriglyceridemia (type V), LCAT activity was lower than in type IV hyperlipoproteinemia. LCAT activity was not changed significantly in type II-a hyperlipoproteinemia. A striking parallel was noted between plasma LCAT and serum pseudocholinesterase activity. It suggested that both these liver secretion enzymes might be induced by an accelerated turnover of serum lipids and lipoproteins. Pathogenical implications of these findings are briefly discussed.
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PMID:Similar behaviour of lecithin:cholesterol acyltransferase and pseudocholinesterase in liver disease and hyperlipoproteinemia. 64 66

The kinetic constants k2, KQ and the second-order rate constant ki of butyrylcholinesterase (acylcholine acylhydrolase, EC 3.1.1.8) inhibition by organophosphorus compounds (C2H5O)2P(O)SX, with both ionic and non-ionic substituents X, were determined at 25 degrees C and pH 7.5 in 0.15 M KCl. The data were analysed in terms of structure-activity relationships and the roles of the leaving group inductive effect and hydrophobicity in the enzyme specificity were established. This made possible calculations of the actual contribution of the substituent ionic charge in the effectivenes of butyrylcholinesterase action. On the basis of the structure-activity relationships for butyrylcholinesterase and acetylcholinesterase the specificities of the enzymes are compared and some common features are discussed.
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PMID:Leaving group effects in butyrylcholinesterase reaction with organophosphorus inhibitors. 68 29

Acetylcholinesterase (AchE) is reported to have a narrowly restricted distribution among human tissues. Three strains of human fibroblasts which are trisomic for chromosome 2 had an average level of AchE activity over 28 times higher than the average level in 19 control strains of human fibroblasts. In contrast, the mean pseudocholinesterase activity of the trisomy-2 strains did not differ appreciably, or significantly, from the mean for the control strains. The 19 control strains included 10 strains trisomic for autosomes other than 2, and 9 euploid strains. Our estimate of the mean AchE activity in the control strains did not differ significantly from zero and might, in any case, have originated from a minute amount of activity contributed to the cells by an esterase in our culture medium. Despite the striking elevation of AchE activity in fibroblasts trisomic for chromosome 2, extracts of these cells had only about 1.5% of the specific AchE activity (per microgram DNA) present in extracts of human cerebral cortex. None of the 22 strains studied had detectable activity for two other enzymes which, like AchE, have a restricted distribution among human tissues: xanthine oxidase and choline acetyltransferase.
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PMID:Evidence for a striking increase in acetylcholinesterase activity in cultured human fibroblasts which are trisomic for chromosome two. 69 21


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