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)

Cholinesterase activities were measured in plasma (ChE) and in intact erythrocytes (AChE) in patients suffering from manic-depressive illness, their first degree relatives who were well, and unrelated normal volunteers. All the subjects were in a normal mood state at the time of testing. Plasma cholinesterase activity was found to be significantly lower than normal in bipolar (BP), unipolar (UP), other affective disorder (OA) and well subjects belonging to manic-depressive families. Intact erythrocyte cholinesterase (true cholinesterase) activity was also found to be significantly lower than normal in all the above mentioned patients and their relatives. Half of the BP subjects were on lithium treatment and their cholinesterase activities were similar to those patients not on lithium treatment. The data suggest a significant role of cholinergic mechanisms in the etiology of manic-depressive illness.
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PMID:Cholinesterases in primary affective disorders. 405 43

Redistribution of axonal enzymes as a function of time in vitro was studied in an unbranched segment of frog sciatic nerve. Cholinesterase activity moved peripherally at a rate of 99 mm/day and centrally at 19 mm/day. One-quarter of the total nerve content of the enzyme was estimated to be in motion, one-eighth in each direction. Mitochondrial enzymes (hexokinase and glutamic dehydrogenase) moved peripherally at 20-31 mm/day, centrally at 11-20 mm/day. Only 10% of the total content of these mitochondrial enzymes was in motion. No movement of choline acetylase or 6-phosphogluconic dehydrogenase activity was seen even after 4 days in vitro. However, in a 12 day in vivo experiment choline acetylase moved toward the periphery at a rate of 0.34 mm/day. After a day or so in vitro the distal accumulations of cholinesterase and glutamic dehydrogenase decreased, with a concomitant and quantitatively equivalent increase in enzyme activities at the proximal end of the nerve. It is postulated that during incubation a mechanism for reversing the direction of flow develops in the peripheral stump of the nerve. Vinblastine inhibited central and peripheral flow of both cholinesterase and glutamic dehydrogenase. Movement of cholinesterase was not affected by ouabain, thalidomide, or phenobarbital, nor by K(+) excess (110 mM) or absence.
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PMID:Transport of axonal enzymes in surviving segments of frog sciatic nerve. 411 99

1. Cholinesterase staining of rat and guinea-pig extraocular muscle shows focally and multiply innervated fibres.2. The distribution of cholinesterase activities in the populations of focal endings (from singly innervated fibres) and fine motor endings (from multiply innervated fibres) was determined by a sensitive radiochemical method.3. Focal endings had a greater cholinesterase activity than fine motor endings.4. It is suggested that this difference in enzyme activities is related to the functional difference between twitch and slow fibres in extraocular muscle.
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PMID:A quantitative study of cholinesterase in myoneural junctions from rat and guinea-pig extraocular muscles. 417 40

A relatively simple method is described by which cholinesterase was purified about 19000-fold starting from horse serum. Typically 20 litres of serum were processed to yield 15-18mg of electrophoretically pure cholinesterase in the form of an active salt-free dry powder. The method included two stages: fractionation with (NH(4))(2)SO(4) and ion-exchange chromatography. The (NH(4))(2)SO(4) stage included, in principle, the acid (pH3) step of the Strelitz (1944) procedure. The step took advantage of the stabilizing effect that 33%-satd. (NH(4))(2)SO(4) has on cholinesterase activity at pH3 and it is recognized that in the absence of (NH(4))(2)SO(4) the enzyme is rapidly destroyed at pH3. Cholinesterase was significantly more stable to pH3.0 at 2 degrees C than at 24 degrees C, and the acid step was done at both temperatures. The specific activities of the final products obtained by way of acid steps were the same at either temperature, thus indicating that the step has not harmed the enzyme active sites. The product from the first two stages was purified over 18000-fold and was 85-90% cholinesterase. The remaining impurities were removed by preparative gel electrophoresis. The product was about 40% more active and contained 40% more active sites per unit weight than electrophoretically pure cholinesterase prepared from partially purified commercial starting material. Although the number of active sites per molecule was not determined with certainty, a value of at least 3 and possibly 4 was indicated. The partial specific volumes were determined with a precision density meter, on the ultracentrifuge and from the amino acid and carbohydrate composition. The values by these independent methods were 0.688, 0.71 and 0.712ml/g, respectively. The amino acid and carbohydrate composition was determined. The cholinesterase contained 17.4% carbohydrate including 3.2% N-acetylneuraminic acid.
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PMID:The purification of cholinesterase from horse serum. 446 52

1. An enzyme similar to mammalian acetylcholinesterase is found in high activity in the nervous tissue of Palaemonetes varians, i.e. eyes plus stalks, brain, suboesophageal ganglion and ventral cord. Acetylcholinesterase is also found associated with the abdominal muscles. Multiple enzyme forms are found in extracts of nervous tissues and muscles by electrophoresis and isoelectric focusing. 2. Cholinesterase is present in high activity in the stomatogastric system of P. varians. Three electrophoretically separable forms are found, having isoelectric points at pH4.2, 4.5 and 5.4. 3. Approx. 50% of the total acetylcholinesterase activity, approx. 80% of the choline acetyltransferase activity and 100% of the acetylcholine equivalents are found associated with the nervous tissue. Among the tissues examined, eyes plus stalks were the richest source of both choline acetyltransferase and acetylcholine equivalents. Suboesophageal ganglion and brain also contained large amounts of these components. 4. The distribution of these components could support the function of acetylcholine as a central and/or sensory transmitter in P. varians.
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PMID:Some components of the cholinergic system in the prawn Palaemonetes varians (Leach). 477 68

Cholinesterase (ChE) activity is present in crustacean muscle extracts. However, since acetylcholine (ACh) is not a neuromuscular transmitter in these animals, the role and exact localization of ChE was unknown. The histochemical localization of the enzyme was studied in whole muscle and in the sarcoplasmic reticulum fraction of the extract, 50-microm frozen sections of glutaraldehyde-fixed crayfish tail flexor muscle were incubated with acetylthiocholine (ATC) as substrate, and examined under the electron microscope. After some modifications in published techniques, dense deposits were found associated with the sarcolemma, sarcolemmal invaginations, and transverse tubules. No deposits were found in 10(-4) M eserine, or if butyrylthiocholine (BTC) was substituted for ATC. The vesicles in the sarcoplasmic reticulum fraction which demonstrate the activity must represent minced bits of these membranes. Using a spectrophotometric method, the kinetics of the crustacean muscle enzyme was compared to the acetylcholinesterase (AChE) on mammalian red blood cells and in the lobster ventral nerve cord. Surprisingly, and contrary to previous reports, the crustacean muscle enzyme did not demonstrate substrate inhibition. While a number of similarities to AChE were found, this lack of substrate inhibition makes questionable an unequivocal similarity with classical AChE.
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PMID:Localization and properties of the cholinesterase in crustacean muscle. 480 7

Cholinesterase activity of brain and content of growth hormone and prolactin in the pituitary were compared after short-term (3 days) and long-term (14 days) treatment with paraoxon in male and female rats. Within 3 days cholinesterase activity was reduced to between 5 and 15 percent of that in controls. The content of growth hormone in the pituitary was increased in long-term experiments by 50 percent. This increase in paraoxon-treated animals-suggests a possible role of a cholinergic mechanism in the regulation of growth hormone secretion.
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PMID:Paraoxon: effects on rat brain cholinesterase and on growth hormone and prolactin of pituitary. 506 Dec 47

Cholinesterase and succinyldehydrogenase activity of surgically removed left atrial auricles from patients in atrial fibrillation and in sinus rhythm have been compared, using histochemical methods. Higher cholinesterase and lower succinyldehydrogenase activity has been found in atrial fibrillation than in sinus rhythm. The pulmonary capillary mean pressure of patients with atrial fibrillation and sinus rhythm have been also compared. There was no significant difference between the two groups. On the basis of the reported examinations, it is not possible to decide whether the changes in enzyme activities are the cause or the result of atrial fibrillation.
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PMID:Changes of myocardial enzyme activities in atrial fibrillation. 521 48

Cholinesterase inhibitors that can pass the blood-brain barrier produce hypothermia when injected intravenously in just sublethal doses. From a comparison of the hypothermia-reducing effects of five cholinesterase-reactivating oximes when injected intraperitoneally or subarachnoidally into rats pretreated with DFP or soman it was possible to distinguish central and peripheral actions of the oximes. The comparative efficacy of the five oximes and the effectiveness of cholinesterase inhibitors in producing hypothermia in other animal species, including man, are discussed.
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PMID:The anticholinesterase hypothermia in the rat: its practical application in the study of the central effectiveness of oximes. 531 45

Cholinesterase was purified from human serum by a three-stage procedure involving chromatography on DEAE-cellulose at pH4.0, an electrofocusing technique and gel filtration on Sephadex G-200. The final product was purified 13000-fold with a yield of 54%, and only one protein and one cholinesterase band could be demonstrated by polyacrylamide-disc electrophoresis. The catalytic properties appeared to be unchanged by the purification procedure. The molecular weight was determined by both ultracentrifugation in a density gradient and gel filtration, and values close to 366000 were obtained. The isoelectric point of cholinesterase was estimated to be pH3.99. The method appears suitable for the preliminary purification of the rare genetic variants of human cholinesterase.
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PMID:Purification and properties of human serum cholinesterase. 544 75


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