Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.8 (cholinesterase)
12,691 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We estimated the concentrations, multiple forms, and lectin binding of five microsomal enzymes in particle free extracts from human kidney, pancreas, jejunal mucosa, and normal and cancerous liver. While arylesterase markedly reacted only with concanavalin A, arylamidase, alkaline phosphatase, gamma-glutamyltransferase, and cholinesterase were intensely precipitated by lectins from Ricinus communis 120, Canavalia ensiformis, Triticum vulgare and Phaseolus vulgaris S. Agglutinins from Glycine max, Arachis hypogaea and Ulex europaeus proved less effective. The reaction mainly depended on the origin of enzymes not on their species. Desialylation always decreased precipitation, and in extracts of normal liver parenchyma it even totally abolished precipitation, by Triticum vulgare lectin. Sialoenzymes therefore appear to be normal intracellular constituents. Differences between enzymes from normal and cancerous liver were not reflected by variant properties of the corresponding activities in sera. The same held true for multiple forms. The reasons for these differences are discussed.
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PMID:[Catalytic concentration, multiple forms, and lectin affinity of microsomal enzymes from human tissues: lectins as reagents, II (author's transl)]. 612 Feb 6

The activities of serum pseudocholinesterase, lecithin: cholesterol acyltransferase (LCAT) and gamma-glutamyltransferase in rabbits were investigated before and after dichlorvos administration in vivo. The effects of this organophosphate on some serum lipids and lipoprotein fractions were also determined. LCAT activity remained almost unaffected after organophosphate administration. However, serum gamma-glutamyltransferase and pseudocholinesterase activities markedly decreased. Dichlorvos markedly lowered both serum low density lipoprotein (LDL) and cholesterol contents, whereas high density lipoprotein (HDL) concentration increased and very low density lipoprotein (VLDL) remained unaffected. Triglycerides as well as esterified fatty acids increased significantly but the statistical changes in free fatty acid concentrations were not significant, because individual variations in fatty acid concentrations were high.
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PMID:Relationship between serum lipids, lipoproteins and pseudocholinesterase during organophosphate poisoning in rabbits. 614 81

The stability of various marmoset (Callithrix jacchus) plasma constituents was investigated after storage at room temperature, 4 degrees C, and -20 degrees C. The method of sequential analysis ensured that the between-run bias of the methods of analysis used was drastically reduced, and the definitions of stability were linked to the imprecision of these methods. Optimal conditions for storage for as long as 48 h depended on the analyte being measured. Room temperature was optimal for cholinesterase and acetylcholinesterase; 4 degrees C for protein, albumin, alanine aminotransferase, isocitrate dehydrogenase, sorbitol dehydrogenase, lactate dehydrogenase, and glutamate dehydrogenase; and -20 degrees C for glutathione reductase and alkaline phosphatase. For aspartate amino-transferase and gamma-glutamyltransferase, either 4 degrees C or -20 degrees C would be suitable. Reasons are advanced for some conflicting reports in the published work, and we emphasize the need to investigate each analyte and species separately.
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PMID:Stabilities of some constituents of marmoset (Callithrix jacchus) plasma under various conditions of storage. 641 8

Serum pseudocholinesterase in accordance with indicators revealing the lipid metabolism and liver function was studied in rats exposed to phenobarbital, bis-p-nitrophenylphosphate and disulfiram in vivo. Phenobarbital markedly induced the hepatic microsomal drug-metabolizing enzymes and tended to decrease the triglyceride content in serum. Serum lipids remained almost unaffected after the treatment of bis-p-nitrophenylphosphate. However, serum gamma-glutamyltransferase activity showed a marked decrease to this organophosphorus compound. Disulfiram activated the microsomal UDP-glucuronosyltransferase (p-nitrophenol) activity, and caused an enhancement of serum total cholesterol, which suggests that this drug might be atherogenic.
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PMID:Serum lipids and hepatic microsomal enzymes with special reference to serum cholinesterase in Wistar rats. 671 39

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

We studied the effects on 25 analytes of duration of contact of serum with non-anticoagulated blood and of temperature. Serum was separated after blood was allowed to stand, for 0, 2, 4, 6, 8, 24, or 48 h at 4, 23, or 30 degrees C. Results obtained for bilirubin, albumin, zinc sulfate turbidity, thymol turbidity, cholinesterase (EC 3.1.1.8), alkaline phosphatase (EC 3.1.3.1), leucine aminopeptidase (EC 3.4.11.1), amylase (EC 3.2.1.2), total cholesterol, triglycerides, beta-lipoprotein, serum urea nitrogen, creatinine, uric acid, and gamma-glutamyltransferase (EC 2.3.2.2) were not influenced by storage at 4, 24, or 30 degrees C for as long as 48 h. Negligible differences were seen for potassium in sera in contact with cells as long as 24 h at 23 degrees C and for inorganic phosphorus after 48 h at 4 degrees C. However, at 4 degrees C we noted an increase at 8 h, a slight decrease at 30 degrees C. Statistically significant changes were seen for total protein and calcium after 48 h at 30 degrees C; for aspartate aminotransferase (EC 2.6.1.1), and alanine aminotransferase (EC 2.6.1.2), between 8 and 24 h at 23 degrees C and as soon as 6 h at 30 degrees C; for lactate dehydrogenase (EC 1.1.1.27) after 8 h at 30 degrees C and between 8 and 24 h at 23 degrees C; for glucose at 24, 4, or 2 h of storage at 4, 23, or 30 degrees C, respectively; for inorganic phosphorus after 48 h at 23 degrees C or 8 h at 30 degrees C; for potassium after 4 h at 4 degrees C or 24 h at 30 degrees C; and for sodium after 48 h at 4 degrees C or 6 h at 23 or 30 degrees C.
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PMID:Serum-constituents analyses: effect of duration and temperature of storage of clotted blood. 744 20

Information on the stability of serum analytes during storage of serum or whole blood samples is often incomplete and sometimes contradictory. Using a widely available analyser (Hitachi 737/Boehringer), we therefore determined the effects of storage time and temperature on the measured concentrations of the following serum analytes: sodium, potassium, calcium, chloride, inorganic phosphate, magnesium, creatinine, urea, uric acid, bilirubin, cholesterol, HDL- and LDL-cholesterol, triacylglycerols, creatine kinase, aspartate aminotransferase, alanine aminotransferase, gamma-glutamyltransferase, alkaline phosphatase, alpha-amylase, lactate dehydrogenase and cholinesterase. When separated serum was stored at + 9 degrees C for seven days, the mean changes in inorganic phosphate and lactate dehydrogenase exceeded significantly (p < 0.05 or 0.001, respectively) the maximum allowable inaccuracy according to the Guidelines of the German Federal Medical Council; all other quantities were sufficiently stable. In serum at room temperature, inorganic phosphate, uric acid, HDL-cholesterol and triacylglycerols increased continuously, whereas bilirubin, LDL-cholesterol, creatine kinase and aspartate aminotransferase decreased more than the guidelines permit during the storage period (p < 0.05 for aspartate aminotransferase, p < 0.001 for the other analytes mentioned). In whole blood stored for 7 days at + 9 degrees C, only the following serum analytes satisfied the stability requirements of the guidelines: calcium, urea, cholesterol, HDL-cholesterol, LDL-cholesterol, triacylglycerols, creatine kinase, gamma-glutamyltransferase and cholinesterase. When stored at room temperature, only sodium, uric acid, bilirubin, cholesterol, triacylglycerols, aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase, alpha-amylase and cholinesterase were still stable after 3 days. The data collected show that all quantities examined are sufficiently stable for four days in separated serum stored at + 9 degrees C.
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PMID:Storage of serum or whole blood samples? Effects of time and temperature on 22 serum analytes. 762 90

A total of 25 apparently healthy adults (13 men and 12 women), 29.5 years (SD = 3.6 years) of age, served as subjects in a 24-h study conducted in Barcelona, Spain, in the spring of 1990. The group had a homogeneous pattern of meals, activity, and behavior. Six blood samples were collected at 4-h intervals over a single 24-h period beginning at 10:00 h. The oral temperature was measured at 2-h intervals to facilitate an independent biological time reference for the local population being studied. The serum concentration of 12 enzymes of clinical interest were measured in each sample: creatine kinase, creatine kinase 2, alanine aminotransferase, aspartate aminotransferase, gamma-glutamyltransferase, alkaline phosphatase, cholinesterase, lactate dehydrogenase, lactate dehydrogenase 1, 5'-nucleotidase, pancreatic alpha-amylase, and triacylglycerol lipase. We supposed that all experimental data obtained for a quantity came from a single "hypothetical subject" that represented the central tendency of the population and then these data were analyzed for circadian rhythm by single cosinor. A statistically significant circadian rhythm was detected in all quantities studied (p < or = 0.05) except for serum concentrations of pancreatic alpha-amylase and triacylglycerol lipase. The maximum daily rhythmic variation was approximately 10% (interval, 6-14%) for all quantities studied except pancreatic alpha-amylase (2.6%). This rhythmic variation is greater than the analytical variation except for 5'-nucleotidase and pancreatic alpha-amylase. The acrophases for the quantities studied (except that of triacylglycerol lipase) coincide with times near those of the oral temperature acrophase (18:01 local time). The results of this study will doubtless contribute to further documentation of the structure of the human circadian timing system and to establishment of time-qualified reference intervals for a defined group of subjects.
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PMID:Circadian rhythms of serum concentrations of 12 enzymes of clinical interest. 810 Apr 88

alpha 1-Acid glycoprotein, an acute phase reactant synthesised by the liver, has been reported to be increased in neoplastic conditions and reduced in chronic liver disease. We measured serum alpha 1-acid glycoprotein by a nephelometric method in 186 subjects (112 males, 74 females): 55 had mild chronic liver disease (chronic hepatitis and steatofibrosis), 45 cirrhosis, 38 hepatocellular carcinoma, 15 extra-hepatic malignant disease; 33 healthy subjects were used as controls. Analysis of variance demonstrated a significant variability among groups (F = 17.08, P = 0.0000). Higher concentrations of alpha 1-acid glycoprotein were detected in malignant extra-hepatic disease than in all other groups (P < 0.01); concentrations of alpha 1-acid glycoprotein were higher in hepatocellular carcinoma than in cirrhosis (P < 0.01). Multiple regression analysis by groups (dependent variable = alpha 1-acid glycoprotein; group 1 = mild chronic liver disease + cirrhosis; group 2 = hepatocellular carcinoma) showed a significant correlation for both group 1 (r = 0.6264, F = 8.005, P = 0.0000) and group 2 (r = 0.8947, F = 13.643, P = 0.0000). The significant standardised regression coefficients were: cholinesterase, C-reactive protein, gamma-glutamyltransferase and iron (negative) for regression upon group 1; C-reactive protein, alpha 1-antiproteinase, gamma-glutamyltransferase, iron (negative) for regression upon group 2. A difference between the 2 regression equation coefficients was detected (F = 5.209, P = 0.0002).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Increase of serum alpha 1-acid glycoprotein despite the decline of liver synthetic function in cirrhotics with hepatocellular carcinoma. 810 7

Aflatoxin (AF)-contaminated and fumonisin B1 (FB1)-contaminated (culture material from Fusarium moniliforme) diets were fed singly and in combination to growing cross-bred barrows. Six barrows (3 replicates of 2 each; mean body weight, 17.5 kg) per group were fed: 0 mg of AF and 0 mg of FB1/kg of feed (control); 2.5 mg of AF/kg of feed; 100 mg of FB1/kg of feed; or 2.5 mg of AF plus 100 mg of FB1/kg of feed for 35 days. The effects on production performance, serum biochemical, hematologic, immunologic, and pathologic measurements were evaluated. Body weight, gain, and feed consumption were significantly (P < 0.05) decreased by AF and AF plus FB1 diets. The FB1 diet decreased feed consumption, and although body weight was numerically decreased, it was not statistically significant. Aflatoxin increased serum gamma-glutamyltransferase (GGT) activity and total iron concentration and decreased urea nitrogen concentration and unsaturated iron-binding capacity. The FB1-alone diet increased serum GGT activity, whereas the AF plus FB1 diet increased serum aspartate transaminase, cholinesterase, alkaline phosphatase, and GGT activities, increased RBC count, triglycerides, and total iron concentrations, and decreased unsaturated iron-binding capacity and urea nitrogen concentration. For the most part, the effects of the AF plus FB1 diet on body weight and hematologic measurements could be considered additive. However, the effect of the AF plus FB1 diet on cholinesterase and alkaline phosphatase activities was greater than additive and was a synergistic response. One pig in the FB1-diet group and 2 pigs in the combination-diet group died. Postmortem lesions in pigs of the FB1-diet group consisted of ascites and increased liver weight. Observations at necropsy for pigs of the AF plus FB1-diet group consisted of hydrothorax, ascites, pulmonary edema, gastric erosions and ulceration, and increased liver and spleen weights. The AF diet increased relative liver weight and resulted in liver that was pale, rubbery, and resistant to cutting. Histologic lesions consisted of hepatic necrosis or degeneration, or both, with variable degrees of bile duct proliferation in barrows of the AF-diet groups. Renal tubular nephrosis was observed in barrows of the FB1-diet group, but this was not consistent in the AF plus FB1-diet group. Cell-mediated immunity, as measured by mitogen-induced lymphoblastogenic stimulation index, was decreased in barrows of the AF and FB1-diet groups, and values in barrows given the combination diet were significantly decreased from those in barrows given the single toxin diets. It was concluded that AF and FB1 (from culture material), singly or in combination, can adversely affect clinical performance, serum biochemical, hematologic, and immunologic values and induce lesions in growing barrows. For most of the variables we evaluated under our study conditions and dosages of toxins, measurements were affected more by the combination diet than by either single toxin diet, and the toxic responses could be described as additive or more than additive, particularly for induction of liver disease.
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PMID:Influence of aflatoxin and fumonisin B1-containing culture material on growing barrows. 859 31


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