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)

Commercially available and affinity-purified butyrylcholinesterases isolated from human serum were examined for their esterasic activity and their ability to hydrolyze various neuropeptides, including neurotensin, substance P, and leucine-enkephalin. The three pools that displayed the lowest esterasic activities were shown to hydrolyze neurotensin with the same HPLC degradative pattern. By contrast, noticeable qualitative and quantitative discrepancies were observed when hydrolyses of substance P and leucine-enkephalin by these three butyrylcholinesterase pools were studied. The pool that exhibited the highest esterasic activity appeared to be homogeneously constituted by 90- and 180-kDa protein bands by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis and was totally unable to hydrolyze these three neuropeptides. This suggested that the three other butyrylcholinesterase preparations could be contaminated by exogenous peptidases. This was confirmed by means of three distinct monoclonal antibodies directed toward human serum butyrylcholinesterase. The three IgG-purified fractions precipitated the esterasic activity, whereas they failed to precipitate the neuropeptide-hydrolyzing activities whatever the substrate examined. Altogether, these results demonstrate that peptidases associated with butyrylcholinesterase are contaminating enzymes that cannot be considered as intrinsic activities of this enzyme.
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PMID:Monoclonal antibodies allow precipitation of esterasic but not peptidasic activities associated with butyrylcholinesterase. 169 18

A report is given on a 66-year-old man suffering from serum cholinesterase anenzymia. The following tests were performed to characterize the genetic pseudo-cholinesterase variants: plasma cholinesterase activity using benzoyldicholine as substrate (according to Kalow) and dibucaine and sodium fluoride as inhibiting substances. In addition, polyacrylamide density gradient gel electrophoresis followed by esterase staining technique (Mascall) was used for the electrophoretic separation of cholinesterase isoenzymes. Similarly, the only daughter's and the granddaughter's sera were analyzed. Determination of activity and inhibitor numbers indicated that the propositus had the homozygote "silent gene" genotype (A = 2, DN = 0, FN = 0). The granddaughter showed an isoenzyme constellation within normal ranges (A = 128, DN = 80, FN = 58); for the daughter apparently normal values were also found for activity and inhibitor numbers (A = 73, DN = 82, FN = 58). Figure 1 shows the results of electrophoretic separation from the sera tested and Fig. 2 results obtained by densitometric assessment. Electrophoretic separation and the zymogram obtained from the propositus' serum show only sample peak and albumin fractions. In contrast, the granddaughter's serum turned out to be absolutely normal. In the daughter's sample, however, three cholinesterase components normally found in serum were missing, as also shown by densitometry. Despite apparently normal activity and rather insignificant inhibitor numbers, gradient gel electrophoresis clearly revealed her to be a heterozygote carrier of the silent gene Es variant. As our data are in accordance with results obtained by other investigators, this observation cannot be regarded as exceptional.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[A case of serum cholinesterase anenzymia]. 175 35

Biochemical components usually evaluated in seminal plasma are lower than those in blood serum. In this study the concentration of different constituents in seminal plasma has been analyzed: creatinine, urea, glucose, uric acid, sodium, potassium, triglycerides, cholesterol, bilirubin, alkaline phosphatase, glutamic oxalacetic transaminase (SGOT), glutamic pyruvate transaminase (SGPT), cholinesterase, creatin phospho chinase (CPK), gamma glutamyl transpeptidase, lactic dehydrogenase (LDH), proteins, in comparison with the concentrations of the same constituents in blood. With the exception of uric acid, all the biochemical components in the seminal plasma were either significantly higher or lower than in blood serum, an index of the complexity of the mechanism regulating the presence and distribution of the single components in seminal plasma compared with blood serum. Isoelectro-focussing for proteins showed, in seminal plasma, a higher quantity of fragments and a different distribution of this in comparison with blood serum.
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PMID:[Prospectives of the study of seminal fluid in the diagnosis of infertility]. 178 5

Various 4-arylthiomethyl-2-oxo-1,3-dioxole derivatives IIIa-o were synthesized. Their hydrolysis rates by arylesterase (EC 3.1.1.2) and cholinesterase (EC 3.1.1.8) in human serum were evaluated. Some of them were not hydrolyzed by cholinesterase, but were hydrolyzed easily by arylesterase. Among the substrates, sodium 4-((5-methyl-2-oxo-1,3-dioxol-4-yl)methylthio)benzenesulfonate (IIIg) was selected for its substrate reactivity toward arylesterase and its good water solubility. In addition, neither aliesterase (EC 3.1.1.1), acetylesterase (EC 3.1.1.6) nor cholesterol esterase (EC 3.1.1.13) hydrolyzed the compound. IIIg is thus concluded to be a specific substrate for arylesterase. Our assay system for serum arylesterase using IIIg can be readily applied to an automatic analyzer in the diagnosis of liver cirrhosis.
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PMID:2-Oxo-1,3-dioxoles as specific substrates for measurement of arylesterase activity. 193 62

1. Carbaryl, a carbamate used as a pesticide, increases the short-circuit current (SCC) across the isolated frog skin in a dose-dependent manner. 2. This effect is due to the stimulation of sodium absorption and chloride secretion. 3. Carbaryl action on short-circuit current is unrelated to its inhibitory power on cholinesterase; this statement is supported by two experimental results: (a) carbaryl is equally active on both sides of the skin, (b) atropine pretreatment does not inhibit the carbaryl action on SCC.
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PMID:Actions of carbaryl on the ionic transport across the isolated skin of Rana esculenta. 198 45

The biochemical changes of the elements of cholinergic neurotransmission (choline acetyltransferase, ChAT; acetylcholinesterase, AChE; butyrylcholinesterase, BuChE; and muscarinic cholinergic receptors, mAChR) as well as the electrolyte content were studied in ischemic lumbar spinal cord segments of newborn pigs. Ischemia was elicited by ligating the aorta for 30 min. Although no significant changes were observed in the sodium, potassium and calcium content of ischemic spinal cords, the calcium content was slightly elevated, to 119.3% of the control value. Whereas significant depletions were observed in both AChE and ChAT activities (to 69.1 and 87.7% of the control value, respectively), there was no significant change in BuChE activity as compared to the control value. The mAChR were also decreased, from 33.25 +/- 2.2 to 27.18 +/- 1.9 fmol/mg protein, while the Kd value was not significantly altered. It is concluded that even a relatively brief interruption of the oxygen supply can cause severe damage in the lumbar spinal cord of the newborn pig, affecting the cholinergic neurotransmission elements. This animal model might be suitable for studying the effects of hypoxia in newborns and children during chest operations involving the descending aorta.
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PMID:Effects of ischemia on cholinergic neurotransmission and electrolyte content in newborn pig lumbar spinal cord. 215 20

Using chromatography on DE-52 and acetylcholine-Affi-Gel columns, nicotinic acetylcholine receptor was purified to approximately 10,000 fold from Lubrol extract of rat brain with a recovery of 15%. The purified preparation contained no cholinesterase activity. alpha-Bungarotoxin did not inhibit [3H]acetylcholine binding to the purified preparation. Sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed 4 major protein bands with apparent molecular weights of 53,000, 67,000, 80,000 and 108,000. When nicotinic acetylcholine receptor was eluted with either carbachol or nicotine from the affinity column, these major bands were found on SDS-PAGE gels. Immunoblot analysis showed that the Mr 80,000 protein was an acetylcholine-binding subunit and that the Mr 48,000 protein, a minor band on SDS-PAGE gel, was a structural subunit.
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PMID:Affinity purification of nicotinic acetylcholine receptor from rat brain. 215 81

In the substantia nigra, acetylcholinesterase may have a non-classical function unrelated to cholinergic transmission. Acetylcholinesterase is released from the dendrites of dopamine-containing nigrostriatal neurons and has a subsequent action on these cells, independent of hydrolysis of acetylcholine. The aim of this study was to explore further the precise nature of this "non-cholinergic" action of acetylcholinesterase. Acetylcholinesterase was pressure-ejected in the vicinity of the dendrites of putative nigrostriatal neurons in vitro, in near-physiological amounts, and the effects of this treatment on neuronal membrane properties were investigated. It was found that acetylcholinesterase reversibly hyperpolarized the nigrostriatal cell membrane independent of sodium and calcium channel blockade. Acetylcholinesterase pretreated with an irreversible inhibitor (Soman) of its classical catalytic site produced the same hyperpolarizing effect: however, butyrylcholinesterase, which hydrolyses acetylcholine, was inefficacious. These effects persisted in the presence of the dopamine receptor antagonist sulpiride. It is suggested the acetylcholinesterase can facilitate the generation of a long-duration conductance, which enhances the firing of nigrostriatal cells if the neuron is first hyperpolarized. Hence the action of acetylcholinesterase would be to modulate inputs. These actions are independent of direct interaction with acetylcholine and dopamine systems. Hence, in the substantia nigra, acetylcholinesterase might serve as a "neuromodulatory" secretory protein.
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PMID:Pressure ejection of acetylcholinesterase within the guinea-pig substantia nigra has non-classical actions on the pars compacta cells independent of selective receptor and ion channel blockade. 246 38

Individual insect muscle fibers, whose neuromuscular junctions have been stained with a modification of Ranvier's gold chloride method, can be dissected free and mounted whole if the muscle is prefixed in aldehydes. The neuromuscular junctions along the length of the individual fibers are well delineated and can be measured and counted. Effective procedures include fixation with glutaraldehyde buffered to low pH with sodium citrate, or glutaraldehyde and paraformaldehyde combined in phosphate buffer at neutral pH, followed by exposure to citric acid and to gold chloride. The method is convenient, and could be useful for the study of arthropod neuromuscular junctions in general, since their nerve terminals do not release acetylcholine as a transmitter and cannot be stained by the more commonly used cholinesterase methods.
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PMID:The use of gold chloride to stain developing and adult neuromuscular junctions in the insect. 248 93

Blue-green algae toxins include (1) hepatotoxic peptides that are known to be toxic to cattle, dogs, swine, waterfowl, and sometimes other species; (2) a nicotinic agonist neurotoxin that appears to be toxic to a wide range of animal species; (3) a peripheral-acting cholinesterase inhibitor that is very toxic to swine, birds, and dogs; (4) toxins that impair nervous transmission by blocking sodium channels in nerve cells; and (5) lipopolysaccharide endotoxins. This article provides current information on the mechanisms of action of the primary toxins recognized to date as well as on procedures important in the diagnosis and management of some of the more common cyanobacterial toxicoses in livestock and waterfowl.
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PMID:Algae intoxication in livestock and waterfowl. 250 41


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