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)

The present report incorporates the histochemical mapping of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) among the various nuclei and fiber tracts of the diencephalon and mesencephalon of Calotes veriscolor. The various nuclei, for both enzymes, present varying degrees of staining, ranging from negative nuclei, on the one hand, to mild and intense staining on the other hand. Almost all of the fiber tracts reveal intense activity in BChE preparations, while they demonstrate mild and moderate activities for AChE. The nature of the various nuclei in relation to enzymatic patterns is discussed.
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PMID:Topographical distribution of acetylcholinesterase and butyrylcholinesterase in the diencephalon and mesencephalon of the garden lizard (Calotes versicolor). 59 96

The acetylcholinesterase (AHhE) activity in the corpora lutea of ovaries from sheep has been examined at different stages of pregnancy and the oestrous cycle, by both quantitative and histochemical techniques. The enzyme activity rose during the early part of pregnancy and then levelled out; it appeared to fall sharply at term. During the oestrous cycle the AChE activity was much lower but showed time-related changes. A few results from pigs and cows are included. The cows corpora lutea, unlike those of the sheep and pig contained butyrylcholinesterase (BuChE) as well as AChE. The results are discussed in terms of the possible function of non-neuronal cholinesterases.
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PMID:Cholinesterase activity in the corpus luteum of the sheep and pig. 61 77

Sections of ovary from plains viscacha, cat, ferret, rabbit, rat, guinea-pig and roe deer have been histochemically processed to demonstrate acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) in nervous and non-nervous tissue. The effects of different reproductive states on enzyme activity were observed in some animals. AChE-containing nerves were sparse in rabbit and rat but plentiful in cat and roe deer. Nerves containing BuChE were not detectable in ferret or guinea-pig and were rare in cat. Species variations in the activity and type of enzyme were also found in non-neuronal tissues. Some blood vessels in the ovaries of guinea-pig and viscacha contained AChE. No other species showed a reaction for AChE in non-neuronal stromal tissue but BuChE was present at this site in all animals except rat. Granulosa cells reacted for AChE only in cat and rabbit while luteal cells were reactive in cat, rabbit and roe deer. Some BuChE activity was present in granulosa and or luteal cells in all species except roe deer. In rat, BuChE activity in luteal cells increased during pregnancy and the early phase of pseudopregnancy. The difficulty of assigning a function to ovarian cholinesterases is discussed.
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PMID:Species variation in the distribution of cholinesterases in the ovary of the plains viscacha, cat, ferret, rabbit, rat, guinea-pig and roe deer. 62 Nov 63

The molecular weight of butyrylcholinesterase from horse blood serum was determined using the method of analytical ultracentrifugation. The molecular weight of the enzyme subunit was also determined by its mobility in gel containing sodium dodecyl sulphate. The number of active sites was determined by titrating butyrylcholinesterase with a specific inhibitor, namely di-isopropyl phosphorofluoridate. A conclusion is made that butyrylcholinesterase is a tetramer with one active site per unit.
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PMID:[Quaternary structure of butyrylcholinesterase from horse blood serum]. 62 6

Albino rats were kept for a year under conditions of everyday motor loading or of a constant hypokinesia. An increase of the motor activity results in rise in the acetylcholinesterase activity determined in the synaptosomal and purified mitochondrial fractions while hypokinesia induces a pronounced decrease in this enzyme activity. The butyrylcholinesterase activity somewhat decreases in the synaptosomal fraction after hypokinesa but does not change under the motor loading regime. Motor loading causes an increase in the amount of synaptosomal water-soluble proteins possessing an intermediate electrophoretic mobility and seem to correspond to the brain-specific protein 14-3-2. In the synaptosomal fraction the amount of membrane proteins with a low electrophoretic mobility and with the cholinesterase activity rises. Hypokinesia, on the contrary, decreases the amount of these membrane proteins.
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PMID:[Effect of motor regimes on water-soluble and membrane proteins and cholinesterase activity in subcellular fractions of rat brain tissue]. 62 7

The salient features of this method for biological monitoring of occupational exposure to organophosphorus insecticides are: (a) acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) are determined separately in whole haemolysed blood using specific substrates at appropriate concentrations; (b) 20 microliter of blood drawn from the finger tip is sufficient for both determinations; (c) the blood sample is immediately diluted with a solution of saponin and may thereafter be frozen for storage; (d) diagnostic kits, commercially available for the determination of plasma BuChE, may be employed with modifications; (e) the kinetic procedure is avoided by blocking the enzyme reactions at the end of the incubation period. This paper describes attempts to achieve optimal conditions for the two reactions. Under the conditions finally chosen, the whole blood 'AChE' activity value still includes a small percentage of plasma BuChE activity (12.5% of the total), while the whole blood 'BuChE' activity includes a small percentage of erythrocyte AChE activity (7% of the total). Results of determinations performed with this procedure on 172 healthy subjects are reported.
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PMID:A quick and simple method for the routine determination of acetyl- and butyrylcholinesterase in blood. 65 41

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

The influence of lowering the temperature, by 10 degrees C increments, from 37 decrees C to 17 degrees C on the twitch )Pt) and tetanic (Po) tension during direct and indirect stimulation, on presynaptic acetylcholine (ACh) release and on muscle acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) activity were investigated in vitro on the rat's phrenic-nerve-hemidiaphragm preparation. Decreasing the temperature from 37 degrees C to 17 decrees C caused a progressive increase of the isometric Pt to 195.8 +/- 9.6 (S.E. of mean) and 169.6 +/- 2.9% of control with direct and indirect stimulation respectively. This change in temperature also increased twitch duration and time to peak Pt by factors of about 4 and 6 respectively with both direct and indirect stimulation. The Po/Pt ratio did not change significantly between 37 degrees C and 27 degrees C, but dropped sharply between 27 degrees C and 17 degrees C. With direct stimulation tetanus was only maintained in 50% of the experiments at 37 degrees C and in none at 27 degrees C or 17 degrees C. With indirect stimulation tetanus was maintained in all experiments at 37 degrees C and 27 degress C and in none at 17 degrees C. Post-tetanic facilitation was greater with indirect than direct stimulation and at higher than at lower temperatures. Post-tetanic exhaustion, with both direct and indirect stimulation, was only observed at 37 degrees C. Presynaptic ACh release (pmol . g-1 . min-1) at rest and with stimulation rates of 0.1 to 50 Hz decreased by more than 60% as temperature was lowered from 37 degrees C to 17 degrees C. Cooling from 37 degrees C to 17 degrees C caused a similar decrease in the volley output (pmol . g-1 . volley-1) of ACh. Muscle-AChE and BuChE activities decreased by 34 and 52% respectively when the temperature was lowered from 37 degrees C to 17 degrees C. The findings presented indicate that the site of the facilitating effect of cooling on Pt is the muscle fiber. The facilitation is caused by the delay of the relaxation of the contracted muscle, causing prolongation of the active state and increased tension development. The decreased speed of nerve conduction and ACh release caused by cooling adversely affects neuromuscular transmission. This, however, is partially counteracted by decreased muscle-ChE activity and increased sensitivity of the postjunctional membrane to ACh caused by cooling.
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PMID:The influence of temperature on neuromuscular performance. 69 Jun 33

The distributions of acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) in the superior cervical ganglion (SCG) of the cat were determined by electron microscopy (EM) with the bis-(thioacetoxy)aurate (I), or Au(TA)2, method. Before the infusion of fixative, one of the enzymes was selectively, irreversibly inactivated in vivo, as confirmed by light microscope (LM) examination of sections of the stellate ganglion stained by the more specific copper thiocholine method. Physostigmine-treated controls, for inhibition of AChE or BuChE, were stained concomitantly with tissue for enzyme localization by the Au(TA)2 method for EM examination in each experiment. It was concluded that most of the AChE of the cat SCG is present in the plasma membranes of the preganglionic axons and their terminals, and in the dendritic and perikaryonal plasma membranes of the postsynaptic ganglion cells. BuChE is confined largely to the postsynaptic neuronal plasma membranes. Reasons for the discrepancies between the localizations found by the present direct EM observations and those deduced earlier from LM comparisons of normal and denervated SCG are discussed. It is proposed that a trophic factor released by the preganglionic terminals is probably required for the synthesis of postsynaptic neuronal AChE, and that BuChE may serve as a precursor of AChE at that site.
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PMID:Electron microscope localization of acetylcholinesterase and butyrylcholinesterase in the superior cervical ganglion of the cat. I. Normal ganglion. 70 60

Acetyl- and butyryl-cholinesterase activities have been measured biochemically in normal brain tissue, in senile dementia of Alzheimer type and in mental disorders without Alzheimer-type abnormalities. Acetylcholinesterase was significantly reduced and butyrylcholinesterase significantly increased, compared with the normal, in the hippocampus and temporal cortex of the Alzheimer cases. No significant enzyme changes were seen in the other diseases investigated including multi-infarct dementia, schizophrenia and depression. There was no correlation between age and acetylcholinesterase activity, but a significant positive correlation between the butyrylcholinesterase activities with increasing age (60-90 years) was found in the hippocampus. The possible connection between cholinergic system pathology and these cholinesterase abnormalities in Alzheimer dementia is discussed.
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PMID:Changes in brain cholinesterases in senile dementia of Alzheimer type. 70 27


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