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 sensitive method, especially suitable for clinical laboratories, for the routine determination of cholinesterase activities in whole blood is presented. This method is based on the hydrolysis of propionylthiocholine and the spectrophotometric determination of the thiocholine produced by reaction with 4,4'-dithiodipyridine. The reaction product 4-thiopyridone has an absorption maximum at 324 nm, so that measurement in the presence of hemoglobin is possible. Propionylthiocholine is used at the substrate for both plasma butyrylcholinesterase and erythrocyte acetylcholinesterase. These two enzymes, in the relative amounts at which they are present in human blood, split this ester at about the same rate. Consequently, a first determination gives the total activity of which each individual activity is about 50%. A second determination in the presence of a selective inhibitor ("Astra 1397") for plasma butyrylcholinesterase gives the activity of the erythrocyte acetylcholinesterase. The difference between the two values represents the activity of the plasma enzyme. The validity of the method and the reliability of the results were checked with each blood sample in two ways: (1) by determining the activities of whole blood with an earlier gasometric technique which uses blood sample dried on filter paper; and (2) by measuring the activities in separated plasma and erythrocyte hemolysate eith propionylthiocholine as the substrate.
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PMID:A new approach to determining cholinesterase activities in samples of whole blood. 70 74

Necropsy brain tissue from normal (control) patients and patients with depression and dementia was examined for activities of various cholinergic components, and these related to the degree of senile plaque formation and extent of intellectual impairment. Choline acetyltransferase and acetylcholinesterase activities decreased significantly as the mean plaque count rose, and in depressed and demented subjects the reduction in choline acetyltransferase activity correlated with the extent of intellectual impairment as measured by a memory information test; muscarinic cholinergic receptor binding activity remained unchanged with increasing senile plaque formation but butyrylcholinesterase activity increased. The results suggest a close relation between changes in the cholinergic system and Alzheimer's dementia, but the precise role of the system in this disease remains to be elucidated.
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PMID:Correlation of cholinergic abnormalities with senile plaques and mental test scores in senile dementia. 71 62

The distribution of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) has been investigated in a series of sections passing through the medulla oblongata and pons of the squirrel brain. A comparison of the two enzymes has given an interesting picture of their selective localization in the different nuclei. Marked AChE activity has been observed in the cranial nerve nuclei. BChE activity in various nuclei of the medulla oblongata and pons is variable and occurs diffusely between the cells. Possible reasons pertaining to marked variation in AChE and BChE contents of various nuclei and fiber tracts have been discussed.
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PMID:Histochemical mapping of acetylcholinesterase and butyrylcholinesterase in the medulla oblongata and pons of squirrel (Funambulus palmarum). 73 61

Rats fed a vitamin E-deficient diet for 7--8 weeks postweaning showed no change in brain weight or the activity in brain of various enzymes involved in neurotransmitter synthesis and metabolism. Body and muscle weights were markedly reduced. Muscle choline acetyltransferase and acetylcholinesterase activities were significantly elevated on a protein basis, but the total amount of choline acetyltransferase/muscle was essentially normal and total acetylcholinesterase activity was slightly reduced. Total carnitine acetyltransferase and butyrylcholinesterase activities were markedly decreased. The results are quite different from those found in hereditary murine muscular dystrophy and suggest a myogenic etiology for the vitamin E-deficiency-induced condition.
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PMID:Cholinergic systems in muscle and brain in vitamin E-deficient rats. 74 Jan 30

Biochemical and histochemical methods have been used to determine both activity and distribution of choline ester hydrolases in the rabbit liver. Acetylcholinesterase was detected in kupffer cells, predominantly in th centri- and mid-lobular regions. Neither the activity nor the distribution of acetylcholinesterase activity was influenced by the intravenous injection of zymosan or the iron-dextran complex imferon on at dosages known to stimulate reticuloendothelial phagocytic function. Although this finding suggests that acetylcholinesterase is not primarily concerned with the pocesses of phagocytosis, there exists the possibility that reticuloendothelial acetylcholinesterase may have a function in metabolism of phagocytosed lipids and esters. Butyrylcholinesterase was present in both hepatocytes and the intrinsic hepatic nerves. Polarization of hepatocyte butyrylcholinesterase activity was noted; the enzyme activity being most marked in the centrilobular hepatocytes. Hepatocyte butyrylcholinesterase activity was unaffected by the intravenous administration of zymosan or imferon. The intrinsic hepatic nerves were present only in portal tracts and interlobular septa, there being no evidence for the existence of an hepatic parenchymal plexus. These findings by cholinesterase histochemistry were confirmed by controlled neurohistological techniques. The morphological findings suggest that the intrinsic hepatic nerves regulate blood flow through the organ and are possible sensory to the bile ducts.
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PMID:Neuronal and non-neuronal choline ester hydrolases in the rabbit liver. 75 96

Plasma butyrylcholinesterase (BuChE) and red cell acetylcholinesterase (AChE) activity was measured in patients with endstage kidney disease undergoing hemodialysis or renal transplantation. All patients had significantly lower values of BuChE activity than normals. A single hemodialysis did not influence the level of BuChE activity but caused a moderate, though statistically significant increase of red cell AChE activity. Chronic hemodialysis significantly increased BuChE but did not affect AChE activity. After successful renal transplantation a sharp fall of BuChE activity occurred, a completely unexpected finding. This decrease coincided with the administration of large doses of glucocorticoids. Once the dose of these drugs was decreased the activity of plasma BuChE returned toward preoperative values. No similar changes in red cell AChE were seen. The possible effect of the steroid drugs on protein synthesis in the liver is discussed.
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PMID:Plasma and red cell cholinesterase activity in uremic patterns (effects of hemodialysis and renal transplantation). 76 97

The human serum butyrylcholinesterase was rapidly purified with an affinity technique on meta-aminophenyltrimethylammonium-agarose; the ionic strength was 0.25 and the specific elution was achieved with 9-amino-10-methylacridinium. After ion exchange on DEAE-cellulose and molecular filtration, an enzyme purified more than ten thousand times was obtained.
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PMID:[Purification of cholinesterase from human serum by affinity chromatography]. 81 47

The structure and histochemistry of the palmar and plantar skin were studied in four adult male marmosets (two Callithrix jacchus and two Callithrix penicillata). In this skin there exist well-developed epidermal ridges, to which are attached one or two ducts of sweat glands. A thick stratum corneum can be seen in the epidermis, while a distinct stratum lucidum cannot be isolated from the other layers. The stratum granulosum is constituted by one or three layers of cells containing keratohyalin granules. Melanin granulations are mainly concentrated in the basal cells of the epidermal ridges. Dendritic melanocytes and amelanotic melanocytes containing alkaline phosphatase are found among the epidermal cells. Glycogen, UDPG-GT and phosphorylases are mainly present in the middle and lower Malpighian cells of the epidermal ridges. Alkaline phosphatase, ATPase, alanyl amino-peptidase and leucine aminopeptidase were absent in the epidermal cells. SDH, cytochrome oxidase, MAO and a certain number of NAD-dependent dehydrogenases (LDH, ADH, MDH, alpha-GPDH, beta-OHBDH and GDH) showed a stronger reactivity in the basal cells and Malpighian layer. The NADP-dependent enzymes (G-6-PDH, 6-PGDH, cis-aconistase and ICDH) were more reactive in the upper Malpighian layer and stratum granulosum. The stratum corneum showed some acid phosphatase and nonspecific esterase reactivity. The collagenous fibers intertwined with a small number of very thin elastic ones and a larger amount of reticular fibers run almost parallel to the epidermal ridges in the papillary body. In the reticular dermis some fibers are disposed transversely to the epidermal ridges. Meissner corpuscles reactive to butyrylcholinesterase, acetylcholinesterase, nonspecific esterase and G-6-PA are disposed at regular intervals and frequently at each side of the epidermal ridges. Pacinian corpuscles were found only in the hypodermis. The eccrine sweat glands contain glycogen, UDPG-GT and phosphorylase in their secretory, ductal and myoepithelial cells. The secretory part shows a uniform reactivity for every dehydrogenase because it contains only one type of cells (clear cells). The intraepidermal segment of the ducts shows a stronger reactivity to nonspecific esterase and NADP-dependent dehydrogenases than the epithelial cells around it.
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PMID:The skin of the palms and soles of the marmosets (Callithrix jacchus and Callithrix penicillata). 82 86

The behaviour of several dehydrogenases(succino-, beta-glycerophosphate-, lactate-, alcohol-, beta-hydroxibutyric acid-, glucose-6-phosphate-, isocitronic acid-dehydrogenase, monoamino-oxidase, and gamma-aminobutyric acid-transaminase) and of several hydrolytic enzymes (non-specific esterase, lipase, acetylcholin-, butyrylcholinesterase, alkaline phosphatase and leucinaminopeptidase) was investigated in the neurons of NSO and NPV, in the infundibulum and in the neurohypophysis and the innervation of the neurons (acetylcholinesterase, monoamino-oxidase, catecholamines) by unmilked and milked cows. The milking stimulus influences the metabolism especially in the neurosecretory cells of the NPV. After the milking stimulus the activity of oxydative enzymes is above all very increased, the anaerobic way of the output of energy is after that also higher. The building up of the carbohydrates through glycolyse in the neurosecretory cells of the NPV after the milking stimulus is increased. The possible participation of the investigated hydrolytic enzymes on the metabolism of the neurosecretory cells is discussed. The neurons of the NPV were innervated for the most part adrenergic. It is discussed the participation of the enzymes succinodehydrogenase and monoaminooxidase on the hormone release in the neurohypophysis.
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PMID:[Enzymhistochemical investigations on the hypothalamo-neurohypophysial system of unmilked and milked cows (author's transl)]. 82 94

In a model of sheep perorally intoxicated with a 200.0 mg kg-1 trichlorphon dose, the effectivity of the worked out therapeutical procedure was confirmed; the procedure consisted in the administration of an anticholinergic (20.0 mg of 1.1% atropine s. c. pro toto) and cholinesterase reactivator (30.0 mg of 10% trimedoxime kg-1 i. m.) mixture 4 hours after the administration of the noxious agent. A determination of the erythrocytic acetylcholinesterase (AChE, E.C.3.1.1.7.) and plasmatic butyrylcholinesterase (BChE, E.C.3.1.1.8.) activities in the intoxicated sheep should be considered a decisive clinical and diagnostical test for taking veterinary-therapeutical, veterinary-hygienical or veterinary-sanitary measures in intoxications with anti-cholinesterase substances on the whole.
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PMID:[Treatment with antidotes in sheep perorally intoxicated]. 82 2


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