Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.7 (acetylcholinesterase)
28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Spinal ganlia of a 9-day chick embryo were cultivated by the method of "floating rafts" in common medium (control) and in the medium containing amizyl (100 microgram/ml) or a neuregrowth factor (50 microgram/ml). With the action of amizyl there proved to be an increase in the number of surviving neurons; the majority of these neurons contained monoaminoxidase; there was a rise of NAD-diaphorase activity, and, to a lesser extent, of lactic dehydrogenase and isocitric dehydrogenase activities. The neurogrowth factor caused an increase in the number of nerve cells with acetylcholinesterase; there was an elevation of NAD-diaphorase and some rise of malic dehydrogenase activities; the activity of lactic dehydrogenase became maximal; as to succinic dehydrogenase--its activity was somewhat suppressed.
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PMID:[Effect of nerve growth factor and amizil on the viability and metabolism of cultured spinal ganglia]. 56 23

Microwave-stimulated enzyme incubations for acetylcholinesterase, 5'-nucleotidase, alkaline phosphatase, lactate dehydrogenase, malate dehydrogenase, succinic dehydrogenase and isocitric dehydrogenase were studied, and compared with incubations in a waterbath. Temperature settings of 37 degrees C and 50 degrees C were used, and the incubation times were varied from 30 seconds to 30 minutes. The desired temperature of the incubation solution was reached in the microwave oven within 1 minute, whilst in the waterbath it took 10 to 25 minutes. The microscopic results for alkaline phosphatase and succinic dehydrogenase at a temperature setting of 50 degrees C were superior in the microwave method for incubation times less than 15 minutes. It is postulated that the increased reaction product of alkaline phosphatase and succinic dehydrogenase is due to a temperature effect, which has to be large enough to be of practical value. For the other enzymes studied, microwave-stimulated incubations were no better than the conventional incubations at corresponding temperatures. For 5'-nucleotidase there were aspecific lead deposits in the microwave method. All enzymes performed at the elevated, unphysiological temperature of 50 degrees C proved to have advantages, except for 5'-nucleotidase, whilst for malate dehydrogenase there was an aspecific reduction of the colour developer at this temperature.
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PMID:Microwave-stimulated brain enzyme incubations are possible at the unphysiological condition of 50 degrees C. 224 28

The effect of hypoparathyroidism and low blood calcium on enzyme levels in rat liver and kidney is shown. Four animal groups were used: parathyroidectomized (PTX), PTX with CaCl2 added in the drinking water, sham-operated controls and sham-operated with CaCl2 added in the drinking water. PTX significantly lowered serum parathyroid hormone (PTH) and calcium. Supplementation of CaCl2 in the drinking water increased serum Ca levels in PTX rats but not in the controls. Significant changes in several liver and kidney enzymes were seen. Most affected were the liver NADP dependent enzymes, glucose-6-phosphate dehydrogenase and malic enzyme. Similar patterns but with relatively smaller changes were seen in the liver enzymes, lactic dehydrogenase, hexokinase, and aspartate transferase. No significant differences between the groups were seen in the levels of malic dehydrogenase, isocitric dehydrogenase, fructose-6-phosphate kinase and cholinesterase. In the kidney, which was less affected than the liver, the only significant difference was seen in the level of malic enzyme. Serum total lipids in the PTX group were significantly lower. All the changes seen were partially reversed by Ca supplementation in the drinking water.
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PMID:Biochemical change in the liver and kidney of rats following parathyroidectomy. 400 1

The effects of chronic and life-span (i.e. over 2 years) treatment with manganese (1 mg MnCl2.4H2O per ml of drinking water) on a number of neurochemical parameters were studied. In development Mn-treatment led to transient but age-dependent decreases in synaptosomal dopamine uptake in hypothalamus, striatum and mid-brain and decreases in synaptosomal choline uptake in hypothalamus but increase in synaptosomal choline uptake in striatum. However, synaptosomal noradrenaline and serotonin uptake in these brain regions remained unaltered. Mn-treatment in development led to small decreases in choline acetyltransferase activities in cerebellum and mid-brain of 2 month old rats but did not affect the regional distribution of glutamic acid decarboxylase or acetylcholinesterase. The same treatment did not alter regional distribution of NAD-linked isocitric dehydrogenase although treatment with a high dose (10 mg MnCl2.4H2O per ml) resulted in transient but age-dependent decreases in the activities of this enzyme but not those of glucose-6-phosphate dehydrogenase in cerebral cortex and mid-brain. Lifespan Mn-treatment (1 mg MnCl2.4H2O per ml) exerted antagonistic effects on the age-related changes in activities of several enzymes. These results suggest that chronic Mn toxicity selectively affects several neurochemical paradigms and the long-term effects of Mn toxicity on brain development and aging are different.
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PMID:Differences in the neurotoxic effects of manganese during development and aging: some observations on brain regional neurotransmitter and non-neurotransmitter metabolism in a developmental rat model of chronic manganese encephalopathy. 614 83

The accumulations by axoplasmic transport of selected enzyme activities proximal and distal to a ligature placed on the sciatic nerve were monitored in rats exposed in utero to maternal antibodies to nerve growth factor (NGF) and in control rats. Littermates of the animals exposed to anti-NGF were shown elsewhere to have had a 70% reduction in the number of sensory neurons in dorsal root ganglia and a 90% reduction in number of neurons in superior cervical (sympathetic) ganglion. The accumulation of F(-)-sensitive acid phosphatase activity was depressed 75% both proximal and distal to the tie. Accumulation of F(-)-resistant acid phosphatase activity was depressed nearly 50% proximal to the tie. Distal accumulation of this activity did not occur in either group of rats. Accumulation of acetylcholinesterase activity was depressed 30%. Distal accumulation of the activities of beta-glucuronidase and hexokinase was depressed 50%. In the lumbar dorsal root ganglia, dry weight was reduced 40%, and the activities of peroxide-sensitive, F(-)-resistant acid phosphatase and of the mitochondrial enzymes hexokinase, glutamic dehydrogenase, glutamic-oxalacetic transaminase, and NAD-dependent isocitric dehydrogenase were all reduced a little more, 45--50% per ganglion. However, the activities of the lysosomal enzymes, F(-)-sensitive acid phosphatase and beta-glucuronidase, of the peroxide-resistant, F(-)-resistant acid phosphatase, and of the mitochondrial enzyme glutaminase were all reduced about 60% per ganglion. The results of these measurements were interpreted to suggest that much, and perhaps all, of the F(-)-sensitive acid phosphatase activity in motion in peripheral nerve in rat is confined to sensory axons.
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PMID:Transported enzymes in sciatic nerve and sensory ganglia of rats exposed to maternal antibodies against nerve growth factor. 616 7

Activities of 14 enzymes were determined in psoas muscle, smooth muscle, diaphragm, heart, brain, liver, kidney, spleen, pancreas, salivary glands, zygomatic gland, intestinal mucosa, subcellular fractions, and plasma of the dog. In pups, plasma activity of most enzymes was high, except iditol dehydrogenase (ID), glutamate dehydrogenase (GLD), alanine aminotransferase (ALT), aspartate aminotransferase (AST), and D-fructose-1,6-diphosphate aldolase (ALS). Alkaline phosphatase (ALP), ALS, cholinesterase (CHS), creatine kinase (CK), alpha-hydroxybutyrate dehydrogenase (HBD), lactate dehydrogenase (LD), and malate dehydrogenase (MD) decreased significantly (P less than 0.01) with increasing age, but in dogs greater than 7 months, all enzymes except CK, HBD, and ALT revealed reasonably constant plasma values. Enzymes ALT, GLD, CHS, and ID are specific for liver, CK and ALS for muscle, HBD to some degree for myocardium, and alpha-amylase for pancreas. The ALP and gamma-glutamyltransferase were located in microsomes, GLD in mitochondria, MD and AST in mitochondria and cytoplasm, and isocitric dehydrogenase, LD, and the other enzymes only in cytoplasm.
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PMID:Enzyme activities in the dog: tissue analyses, plasma values, and intracellular distribution. 703 2

Enzyme levels in the plasma, liver and heart muscle from normal healthy and round heart diseased (RHD) turkey poults are described. RHD was induced by feeding with furazolidone or developed spontaneously. Lactic dehydrogenase (LDH), isocitric dehydrogenase (ICDH) and creatine-phosphokinase (CPK) were significantly lower in the heart muscle of birds showing RHD symptoms, while liver cholinesterase (CE) was significantly higher in the diseased birds in comparison to the controls. LDH isoenzyme pattern in the heart muscle and liver showed a shift toward the M type tetramers. The significance of these findings is discussed.
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PMID:Biochemical changes in blood and tissues associated with round heart disease in turkey poults. 1876 2

Studying biochemical changes in the blood and liver of geese during cramming showed significant increases in the liver enzymes: malic dehydrogenase (MDH), lactic dehydrogenase (LDH), aspartate aminotransferase (AST) and malic enzyme (ME), and a decrease in alkaline phosphatase (ALP). No significant changes were seen in the activity of isocitric dehydrogenase (ICDH), and glucose 6 phosphate dehydrogenase (G6PDH). There were significant increases in serum ME, ICDH, LDH, MDH, AST, acid phosphatase (ACP), sorbitol dehydrogenase (SDH), and total lipids and decreases in serum ALP, albumin and the haemocrit. No significant changes were seen in the activity of cholinesterase, glucose, total proteins, globulins and inorganic phosphorus. There were good correlations between liver size and the change of some of the biochemical parameters studied, which may serve as markers for the presence and degree of liver fattening. There were differences between families of gray and white geese and concentrations and activities of the blood constituents paralleled the degree of liver fattening. The possibility of using these parameters as genetic markers is discussed. No correlations were found between the liver and serum biochemical parameters. The effect of transporting the geese from the farm to the slaughter house on the levels of the blood constituents is described.
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PMID:Biochemical changes associated with fatty liver in geese. 1876 79