Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P17174 (aspartate aminotransferase)
 14,872 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The proposed system of continuous monitoring of enzyme activities is based primarily on the electrochemical behaviour of thiol compounds, and the experimental equipment is extremely simple. The determination of cholinesterase (EC 3.1.1.8) activity is described. The normal values obtained for men (73.9, s +/- 10.3 microkat/l) and for women (71.1, s +/- 10.2 microkat/l), lie within the usual range of analogous photometric methods. Systems for determination of the activities of alkaline phosphatase (EC 3.1.3.1) and adenosylhomocysteinase (EC 3.3.1.1) are described. The activity of aspartate aminotransferase (EC 2.6.1.1) is determined by a combination of enzyme reactions, in which CoA is released from acetyl-CoA. Analogous procedures are discussed for determinations of alanine aminotransferase (EC 2.6.1.2), lactate dehydrogenase (EC 1.1.1.27), lipase (EC 3.1.1.2), and phospholipase A2 (EC 3.1.1.4) activities, and for determination of substrates, e.g., acetate and carnitine. Possible determinations of an additional 199 enzyme activities and of some of substrates are suggested. By determining electrochemically active groups other than thiols this method becomes almost universally applicable.
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PMID:New system of continuous monitoring of enzyme activities and determination of some substrates. 344 Aug 58

The effect of manganese pretreatment on acute toxicity of fenitrothion (FTH) was investigated in male rats by assessing the degree of enzymatic alterations. Oral administration of FTH (260 mg/kg) markedly inactivated cholinesterase (ChE) and carboxylesterase and elevated the activities of acid phosphatase, alanine aminotransferase and aspartate aminotransferase in different tissues 3 h after dosing. Pretreatment of rats with manganese (10 mg/kg, i.p.) 3 days prior to FTH application (260 mg/kg, p.o.) significantly enhanced these enzymatic changes. The results indicate that inhibition of esterases and elevation in other enzymes induced by manganese are likely to contribute to the increased enzymatic alterations observed following combined treatment.
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PMID:Studies on the interaction between manganese and fenitrothion in rats. 359 Feb 18

1. A variety of biochemical measurements were taken periodically in captive northern bobwhite (Colinus virginianus L.), European starlings (Sturnus vulgaris L.), red-winged blackbirds (Agelaius phoeniceus L.) and common grackles (Quiscalus quiscula L.) to determine whether baseline values remain sufficiently stable throughout the year for general clinical use in the absence of concurrent control specimens. 2. Variables included whole blood hematocrit and hemoglobin, plasma lactate dehydrogenase, alpha-hydroxybutyrate dehydrogenase, aspartate aminotransferase, alanine aminotransferase, creatine kinase, butyrylcholinesterase, alkaline phosphatase, glucose, albumin, total protein, creatinine, urea nitrogen, uric acid, cholesterol, and triglycerides, and brain acetylcholinesterase. Butyryl- and acetylcholinesterase were included because of their specific uses in toxicology. 3. Significant seasonal differences were detected for each of the variables except brain acetylcholinesterase in at least one of the species. Significant species differences were detected during at least one season for all of the variables measured. 4. All species were maintained outdoors, but only northern bobwhites came into reproductive condition and showed sex-differences in the clinical variables during their normal breeding season. 5. It was concluded that reference values for the 18 clinical variables measured could be calculated from our data for adult specimens of the species studied, and that results for one species cannot be extrapolated with certainty to any other species. 6. Estimated normal bounds for each of the 18 variables measured by commonly used clinical procedures are presented for reproductively quiescent northern bobwhites, European starlings, red-winged blackbirds, and common grackles.
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PMID:Seasonal variation in diagnostic enzymes and biochemical constituents of captive northern bobwhites and passerines. 366 39

Using fully mechanized analytical equipment, interference by haemolysis in the determination of 26 clinical chemical parameters was determined quantitatively by adding haemolysate to serum. Haemoglobin concentrations up to 6.6 g/l caused essentially no interference in the following determinations: albumin (immuno-nephelometric), alpha-amylase, calcium, chloride, cholesterol, cholinesterase, creatinine, iron, glucose, glutamate dehydrogenase, uric acid, urea, sodium, inorganic phosphate, total protein, transferrin and triglycerides. In the presence of haemoglobin, erroneously high values were found for: lactate dehydrogenase (haemoglobin higher than 0.2 g/l), aspartate aminotransferase, potassium and acid phosphate (haemoglobin higher than 1.5 g/l), creatine kinase (haemoglobin higher than 2.5 g/l) and alanine aminotransferase (haemoglobin higher than 3.4 g/l). Erroneously low values were found for bilirubin (haemoglobin higher than 0.8 g/l), alkaline phosphatase and albumin (by electrophoresis) (haemoglobin higher than 1.5 g/l) and gamma-glutamyltransferase (haemoglobin higher than 3.0 g/l).
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PMID:Haemolysis as an interference factor in clinical chemistry. 371 97

We measured the activity of carnosinase, a prominent hepatic peptidase, in sera from 69 patients with liver disorders. Mean values (and SDs) for those with liver cirrhosis (17 cases) and hepatoma (seven cases) were 0.51 (0.28) and 0.68 (0.21) mumol/mL per hour, respectively--clearly less than for normal adults: 4.19 (0.95) mumol/mL per hour. Samples from 17 cases of chronic hepatitis also showed moderately decreased activity, 1.41 (0.97) mumol/mL per hour. In contrast, 14 cases of acute hepatitis generally showed values falling within the normal limits: 3.41 (1.97) mumol/mL per hour. Our results for carnosinase correlated with those for cholinesterase (r = 0.70) and with the concentration of albumin in serum (r = 0.59), but not with the activity of either creatine kinase, aspartate aminotransferase, or alanine aminotransferase in serum. Carnosinase values differed more among groups of disorders than did the values for cholinesterase or albumin. Measurement of serum carnosinase activity may be of clinical value in assessing the severity of chronic liver-cell damage, but not in differentiating liver disease from nutritional, muscle, or endocrine disorders.
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PMID:Decreased activity of carnosinase in serum of patients with chronic liver disorders. 373 53

Clinically normal Nubian goats were given the antiprotozoal drug imidocarb at single intramuscular doses of 6, 12, 18 and 24 mg/kg, and the various clinical, biochemical and pathological manifestations were recorded. At a dose of 6 mg/kg the drug produced no change in any of the parameters studied. At higher doses, the drug produced dose dependent changes which included increased heart and respiratory rates, increased defaecation, urination, depression, incoordination of movement, weakness of the hindlegs, recumbency, and finally death. Just prior to death, there was a significant decrease in the number of erythrocytes, and in packed cell volume, and haemoglobin concentration. In plasma there was an increase in the activity of aspartate transaminase, urea and creatinine concentrations and inhibition of cholinesterase activity. The main histopathological changes were associated with hepatic and renal damage. Three goats were pre-treated with atropine sulphate (1 mg/animal) and after one hour given imidocarb intramuscularly at a dose of 12 mg/kg. The changes were similar but much less severe when compared with those in animals given imidocarb alone at the same dose.
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PMID:Some effects of imidocarb in goats. 408 55

Combined enzymodiagnostic program--estimation of total activity of blood serum enzymes aspartate aminotransferase (AST), alanine aminotransferase (AAT), alkaline phosphatase (AP), gamma-glutamyl transferase (gamma-GT), glutamate dehydrogenase (GDH), acetyl cholinesterase (ACE), butyryl cholinesterase (BCE)--was studied to evaluate its diagnostic validity in surgical clinic. In mechanical jaundice of various origin mean values of the enzymatic activities studied as well as the enzymatic coefficients were distinctly altered as compared with control values: AST/AAT, gamma-GT/AST as well as the newer coefficients BCE/ACE, AP/gamma-GT, (formula; see text). The jaundices of tumoral and non-tumoral genesis caused markedly dissimilar alterations in the coefficients AST/AAT and (formula; see text). The data of enzymological analysis may be used for differential diagnosis in jaundices.
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PMID:[Enzyme diagnosis of mechanical jaundice]. 409 Mar 51

The intravenous injection of endotoxins isolated from Escherichia coli serogroups O111 and O78 (2 mg/kg) increased the activities of aspartate transaminase and lactate and sorbitol dehydrogenases in the plasma of six- to 11-week-old chickens during the next 24 h. These changes were compared with those produced by adrenocorticotrophic hormone and beta-methasone and were attributed to tissue damage involving the liver followed by increased enzyme synthesis which may have been induced partly by adrenocortical hormones. Further evidence of liver damage was provided by a fall in the activity of cholinesterase. The alkaline phosphatase activity gave no indication of cholestasis.
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PMID:The effect of Escherichia coli endotoxins and adrenocortical hormones on plasma enzyme activities in the domestic fowl. 624 63

The significance of changes in lymph flow for the extracellular distribution and transport of cellular enzymes and for the level of enzyme activities in plasma was investigated. Specimens of thoracic duct lymph were obtained from an extracorporal lymph shunt in anaesthetized, conscious resting and treadmill exercising dogs (6 km X h-1 for 1 h) The activity of 10 enzymes and of protein content in lymph and plasma were studied, as well as lymph flow, lymphatic transport, and the lymph-plasma ratio of these compounds. Lactate, pH, and blood gases were monitored in venous blood. Lymph flow of 0.80 ml X min-1 in anaesthetized dogs more than doubled (to 1.86 ml X min-1) when the animals were conscious and resting. In anaesthetized dogs lymph enzyme activity was higher only for enzymes of predominately hepatic origin, such as choline esterase (CHE) and alanine aminoferase (ALAT), and was lower for aspartate aminotransferase (ASAT) and aldolase (ALD). In conscious dogs, due to activation of the skeletal muscle "tissue pump", lymphatic transport of enzymes with rather high activity in skeletal muscle, and of protein, is significantly enhanced. Enzyme activities in plasma, however, did not differ between the groups. Lymph-plasma activity ratios higher than one were found for lactate dehydrogenase (LDH), malate dehydrogenase (MDH), ASAT, creatine kinase (CK), ALD, and phosphohexose isomerase (PHI). Exercise stimulated lymph flow up to 4.9 ml X min-1, and increased the lymphatic activities of those enzymes with a lymph-plasma ratio higher than unity, these enzymes increasing in the plasma due to the highly increased lymphatic transport.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Enzyme activities in thoracic duct lymph and plasma of anaesthetized, conscious resting and exercising dogs. 642 59

Aiming at an improvement of the screening of toxic substances in biological materials and environment, the following biochemical indices were studied by means of the Tetrahymena pyriformis as a testing object: total protein, total lipids, glucose, lactate dehydrogenase (E.C.1.1.1.27.), gamma-glutamyl transferase (E.C.2.3.2.2.), aspartate aminotransferase (E.C.2.6.1.1.), alanine aminotransferase (E.C.2.6.1.2.), acetyl cholinesterase (E.C.3.1.1.7.), butyryl cholinesterase (E.C.3.1.1.8.), alkaline phosphatase (E.C.3.1.3.1.), acid phosphatase (E.C.3.1.3.2.) and alpha-amylase (E.C.3.2.1.1.). The study was conducted in the period of the population growth in an experimental medium with the minimum content of nutrients within the 96 hours of cultivation. It has been derived from the results that most of the enzymes are at the top of their activity in the early logarithmic stage of growth, i. e. in the period immediately following the log stage of population growth when the cells are getting ready for intensive division and growth; another peak activity period is the logarithmic growth stage--alkaline phosphatase and acid phosphatase are an exception with the culmination of activity in the stationary stage of population growth.
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PMID:[Selected biochemical indicators in the protozoan Tetrahymena pyriformis]. 644 37


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