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)

Karnovsky and Roots offer to use potassium ferricianide for coloured detecting the products of acetylcholine hydrolysis by cholinesterase. The method is based on the reduction of ferricianide to ferrocianide which forms with copper ions, present in the solution, unsoluble ferrocianide. Some properties of ferricianide ion, however, (stability, large size and great hydratation) make it difficult for the substance to penetrate the native cell membranes. The method by Karnovsky and Roots applied to laminated muscular tissue and to the rat nonfixed whole diaphragm, and to the sections from nonfixed tissue of the cat skeletal muscle verifies space isolation of ferricianide from the enzyme localized at the other side of cell membrane.
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PMID:[Use of potassium ferricyanide in histochemistry]. 64 58

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

Glyoxylic acid-induced fluorescence technique and a copper thiocholine method were used to investigate the ontogenesis of the catecholamine-containing and cholinesterase-positive nerves of the rat iris and cornea. First fluorescent nerve fibres appeared in the iris on the 18th gestation day and in the cornea on the 19th day. A rapid increase in the density of the adrenergic nerve fibres of the iris continued to the age of three weeks, while the number of such fibres were small in the cornea. Acetylcholinesterase-positive fibres appeared both in the cornea and in the iris on the 19th gestation day. Their density increased more rapidly in the iris, especially in the sphincter muscle, than in the cornea. Non-specific cholinesterase activity was localized in the Schwann cells and the reaction was more intense during development than in the nerves of the cornea of adult rats.
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PMID:Pre- and postnatal development of catecholamine-containing and cholinesterase-positive nerves of the rat cornea and iris. 70 17

This paper reports a study of changes in red blood cell enzymes and some serum parameters during and after treatment of protein-calorie malnutrition. The red cell GSH levels were low during the crisis, together with the levels of GSSG:NADPH reductase, GSH:H2O2 peroxidase, aspartate aminotransferase and alanine aminotransferase. After treatment the levels of all these enzymes increased significantly to normal values. Of the serum parameters investigated, significant reduction in the activity of the enzymes cholinesterase, catecholamine oxidase, total proteins, albumin, urea and electrolytes were obvious, and returned to normal values after treatment. Ceruloplasmin activity remained low even after three weeks' treatment and could not be related to copper levels. The results are discussed in relation to anemia and liver damage that may accompany the syndrome.
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PMID:Protein-calorie malnutrition: a study of red blood cell and serum enzymes during and after crisis. 82 Apr 94

Copper and Zinc have been found to be potent inhibitors of pseudo-cholinesterase of human plasma and true-cholinesterase of erythrocytes and rat brain.
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PMID:Metallic ions as negative modifiers of cholinesterase. 87 95

A description is given of an outbreak of equine infectious anaemia (E.I.A.) in Campania [at Naples and Aversa (Caserta)]; it was diagnosed by clinical, pathological and serological examinations (Coggins test). Using the serum of 45 horses with E.I.A. and 11 healthy horses (controls), numerous investigations were carried out on: enzymes, intrinsic coagulation factors, lipids and other substances. The results obtained were very interesting and show that in this disease there are significant increases in many enzymes (LDH, LAP, gamma-GT, CPK, PK and ALD) and copper. Insignificant increases were found in other enzymes (SDH, GLDH, MDH, ICDH, AIP, lysozyme, cholinesterase, GOT and GPT) and also intrinsic coagulation factors, lipid substances (total cholesterol, esterified cholesterol, triglycerides) and glucose. LDH-1-isoenzyme remains unchanged, whilst AcP decreases slightly.
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PMID:Biochemical studies on equine infectious anaemia. 101 May 2

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

We developed a method for detecting activity of axonal cholinesterase (CE) and carbonic anhydrase (CA)--markers for motor and sensory nerve fibers (NFs)--in the same histological section. To reach this goal, cross-sections of muscle nerves were sequentially incubated with the standard protocols for CE and CA histochemistry. A modified incubation medium was used for CA in which Co++ is replaced by Ni++. This avoids interference of the two histochemical reactions because Co++ binds unspecifically to the brown copper-ferroferricyanide complex representing CE activity, whereas Ni++ does not. Cross-sections of the trapezius muscle nerve containing efferent and afferent NFs in segregated fascicles showed that CE activity was confined to motor NFs. Axonal CA was detected solely in sensory NFs. The number of labeled motor and sensory NFs determined in serial cross-sections stained with either the new or the conventional technique was not significantly different. Morphometric analysis revealed that small unreactive NFs (diameter less than 5 microns) are afferent, medium-sized ones (5 microns less than d less than 7 microns) are unclassifiable, and large ones (d greater than 7 microns) are efferent. The heterogenous CE activity of thick (alpha) motor NFs is linked to the type of their motor units. "Fast" motor units contain CE reactive NFs; "slow" ones have CE negative neurites.
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PMID:Axon typing of rat muscle nerves using a double staining procedure for cholinesterase and carbonic anhydrase. 171 70

Acetylcholinesterase (AchE: EC 3.1.1.7) was identified and purified from the hemolymph of the scorpion Heterometrus bengalensis. The purity of the enzyme was determined by polyacrylamide gel electrophoresis (PAGE). The molecular weight of the enzyme, determined by sodium dodecyl sulfate-PAGE, was 80,000. The purified AchE hydrolysed acetylthiocholine iodide, but it did not react with butyrylthiocholine iodide. BW284C51, a specific inhibitor of AchE, strongly inhibited the enzyme. The known inhibitor (tetramonoisopropylpyrophosphortetramide) of pseudocholinesterase did not produce any inhibition of the enzyme activity. The purified AchE of scorpion hemolymph was vulnerable to high substrate concentration. The presence of Cu2+ and Ni2+ reduced the enzyme activity, whereas the metal ion, Sn2+, enhanced AchE activity. Ca2+ produced neither inhibition nor activation. (Na+, K+)-ATPase and Mg2+-ATPase activities were greatly enhanced by the purified AchE.
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PMID:Acetylcholinesterase (EC 3.1.1.7), a neurotransmitter enzyme in scorpion hemolymph. 296 37

The histochemical distribution of pseudocholinesterase was studied in the rat cerebellum using Koelle's copper-thiocholine method. Throughout the cerebellum, pseudocholinesterase is uniformly localized in the endothelial cells of blood vessels and in the cell bodies and processes of the Bergmann glia. In addition, we demonstrate that exclusively in the ventral uvula and in the nodulus (lobules IXc and X of Larsell) pseudocholinesterase is localized in a small subpopulation of Purkinje cells. The cell bodies and dendrites of these labeled Purkinje cells form at least 4 distinct parallel bands extending along the sagittal plane of each of the lobules. Two broad bands on either side of the midline, approximately 800-900 microns wide and composed of 15-20 Purkinje cells have been designated as A bands. Two narrower bands, approximately 160-300 microns wide and composed of 5-7 Purkinje cells, on the lateral aspects of the lobules have been designated as B bands. The unique distribution of pseudocholinesterase in a small and anatomically restricted population of neurons suggests that in the cerebellum this enzyme may play a role in the metabolism of neuroactive substances.
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PMID:Neuronal localization of pseudocholinesterase in the rat cerebellum: sagittal bands of Purkinje cells in the nodulus and uvula. 366 77


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