Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.6.1.1 (aspartate aminotransferase)
21,665 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In women employed in an industrial plant in direct contact with epoxide resins and their hardeners, the following biochemical parameters were determined in blood: total protein, seromucoid, haptoglobin, hemoglobin variants, methemoglobin, alpha1-inhibitor of trypsin, lactate dehydrogenase, aspartate and alanine aminotransferases, alkaline and acid phosphatase, gamma-glutamyl transpeptidase, leucylaminopeptidase, and alanine aminopeptidase. Depending on duration of work, Hb A2 fraction and lactate dehydrogenase increased significantly, and aspartate aminotransferase, acid and alkaline phosphatase activities decreased. In pregnant women, leucylaminopeptidase activity and isozyme of placental alkaline phosphatase were decreased.
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PMID:Evaluation of the influence of epoxide resins and their hardeners on the female body. II. Biochemical studies. 101 94

The activities of aspartate transminase (EC 2.6.1.1), alanine transminase (EC 2.6.1.2), alkaline phosphatase (EC 3.1.3.1), acid phosphatase (EC 3.1.3.2) leucine arylamidase (EC 3.4.1.1), aldolase (EC 4.1.2), lactate dehydrogenase (EC 1.1.1.27), malate dehydrogenase (EC 1.1.1.38) and cholinesterase (EC 3.1.1.7) were measured in serum of male rabbits and albino Wistar rats in dlplicate by means of microliter techniques. Furthermore, the diurnal alterations of enzyme activity were established in 8--10 animals of both species. Aspartate transaminase activity in the serum of rats was found to be significantly higher than in the serum of humans and rabbits, and essentially lower alkaline phosphatase values were obtained from the serum of rabbits in comparison with those found for the serum of humans and rats. Relatively high acid phosphatase and aldolase values as well as a very low cholinesterase activity were found in the serum of rabbits and rats. The mean malate dehydrogenase-activity was found to be twice as high as the mean lactate dehydrogenase, which is the contrary of the situation found in human serum. No significant diural alterations of the examined enzyme activities were established. The differences found between the animal and the human enzyme activities in serum are explained by species-determined peculiarities of metabolism or specific enzyme configuration.
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PMID:[Enzyme activities in serum of rabbits and rats-reference values and circadian alterations. Serum enzymes and factors that influence their activity,I (AUTHOR'S TRANSL)]. 103 68

The activities of glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate: NADP oxidoreductase, G6PD), 6-phosphogluconate dehydrogenase (6-phospho-D-gluconate: NADP oxidoreductase, 6PGD), hexokinase (ATP: D-hexose 6-phosphotransferase, Hx), lactate dehydrogenase (D-lactate: NAD oxidoreductase, LDH). glutamate oxaloacetate transaminase (L-aspartate: 2 oxoglutarate aminotransferase, GOT) and dihydrofolate reductase (DHFR) were measured at 8 a.m. in leucocytes of healthy individuals and patients with chronic myeloid leukaemia (CML), chronic lymphatic leukaemia (CLL), myelofibrosis with myeloid metaplasia and polycythaemia vera. In view of the heterogeneity of the leucocyte populations in these conditions, the enzyme activities were correlated to the number of immature cells in CML and to the percentage of lymphocytes in CLL. No differences in the enzyme activities were found between the white cells of healthy individuals, myelofibrosis with myeloid metaplasia and polycythaemia vera. In CML the activities of all enzymes except GOT correlated directly with the number of immature cells; an inverse correlation with the number of lymphocytes was observed in CLL. GOT was the only enzyme whose activity correlated with the number of lymphocytes in the cell suspension. Furthermore, a significantly higher activity of this enzyme was found in Ficoll-isolated CLL lymphocytes as compared to normal lymphocytes.
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PMID:Blood leucocyte enzymes. II. Activities at 8-9 a.m. in cells of normal subjects, chronic lymphatic leukaemia and chronic myeloid leukaemia patients. 105 70

Because of the difficulties in drawing blood for clinical chemistry in small laboratory animals there exist many methods for sampling blood and the preparation of serum, none of which is generally accepted or well standardised. It was the aim of this study to investigate the effects of sampling techniques on normal values of enzyme activities in the serum of rat and mouse. The activities of the following enzymes were determined: sorbitol dehydrogenase, lactate dehydrogenase, malate dehydrogenase, glutamate dehydrogenase, aspartate aminotransferase, alanine aminotransferase, pyruvate kinase, creatine kinase, myokinase, alkaline phosphatase and leucine aminopeptidase. In addition plasmaproteins, urea and inorganic phosphorus were measured. In rats blood was obtained from the following sites: retroorbital venous plexus, jugular vein, heart and ventral aorta. In mice blood was sampled from the jugular vein and the ventral aorta. Shifts of water from the interstitial to the intravascular space due to hypovolemia occurring during the experimental procedure were followed up by measuring the hematocrit and the distribution of radioiodide labelled albumin. In rats the activities of lactate dehydrogenase, malate dehydrogenase, aspartate aminotransferase, pyruvate kinase, creatine kinase and myokinase found in blood serum obtained from the retroorbital venous plexus and the ventral aorta were too high compared to the other sampling sites. Activities of alkaline phosphatase and alanine aminotransferase were slightly elevated when blood was sampled from the punctured retroorbital venous plexus. Small differences in plasmaproteins and hematocrit values were found to be due to acute shifts of water within the extracellular space. In mice the activities of lactate dehydrogenase, malate dehydrogenase, aspartate aminotransferase and myokinase were found to be too high in blood serum obtained from the ventral aorta. Efflux of enzymes from damaged cells and the interstitial space ive caused erroneous results too, but only to a minor extent. The most reliable method for blood sampling in rat and mouse is the cannulation of the jugular vein. The heart puncture can be recommended too. Attention should be paid, however, to the possibility of aspirating disrupted muscle cells through the inserted needle.
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PMID:[Effects of blood sampling on enzyme activities in the serum of small laboratory animals (author's transl)]. 108 84

1. The effects of protein concentration and ionic strength on the adsorption of the individual glycolytic enzymes to F-actin and F-actin--trypomyosin--troponin have been studied. 2. Appreciable association was demonstrated under conditions of physiological ionic strength and high protein concentration, and tropomyosin--troponin established as an important and generalized component of these interactions. 3. Phosphofructokinase, aldolase, pyruvate kinase, lactate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase and glucose-6-phosphate isomerase were strongly bound under these conditions, while triosephosphate isomerase, phosphoglycerate kinase, phosphoglycerate mutase, enolase and hexokinase displayed less adsorption to the structural proteins. 4. The influence of a number of parameters on the adsorption phenomena was examined. Ca2+ and fructose 1,6-diphosphate increased the adsorption of aldolase, lactate dehydrogenase and pyruvate kinase, while decreasing the adsorption of the enzymes of the constant-proportion group. 5. Of the other major enzymic components of skeletal muscle, creatine kinase, adenylate kinase and malate dehydrogenase showed no adsorption to F-actin--tropomyosin--troponin under the experimental conditions. Some adsorption was evident, however, in the case of aspartate aminotransferase, (NADP) isocitrate dehydrogenase and alpha-glycerolphosphate dehydrogenase. 6. These results have been discussed in relation to their functional significance and the roles of enzyme compartmentation in the cell.
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PMID:On the association of glycolytic enzymes with structural proteins of skeletal muscle. 111 88

A new fast kinetic analyzer, System Olli 3000, is evaluated as an instrument for the routine clinical laboratory measurement of the activities of aspartate aminotransferase, alanine aminotransferase, and lactate dehydrogenase in serum. The System Olli 3000 consists of dispensers for simultaneous multiple dispensing of sample and reagents, incubators, vortex-type shakers, and a photometer with quartz fibre optics connected to a computer, allowing cycling measurements of 24 cuvets 24 times in 2 min. An unique slope search algorithm is described. The system shows a high degree of precision and a wide linearity range; activities of at least 10-fole the normal upper limit for all three of these enzymes can be measured without diluting the serum sample. As many as 380 analyses per hour (including calibration and blanks) can be carried out by one technician. For comparison, enzyme measurements were also made with an LKB 8600 Reaction Rate Analyzer and a Pye Unicam SP 8005 spectrophotometer coupled on-line to an IBM 1800 computer. Results obtained with the different instruments correlated well, especially in the region of main interest, i.e., above the normal upper limit. We conclude that the new instrument has many potentialities in kinetic analyses of nonenzymatic constituents in biological fluids.
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PMID:Evaluation of the new "System Olli 3000" kinetic ultraviolet analyzer for measuring aspartate ana alanine aminotransferase and lactate dehydrogenase activities in serum. 112 12

Glycylprolyl beta-naphthylamidase activities in sera from 40 normal subjects (18-81 years) were: 22.6 +/- 0.9 (S.E.) (11.8-38.2) I.U./1 serum at 37 degrees C. The enzyme activities did not differ significantly with age between the younger group under 40-years-old and the older group over 40-years-old. Males, especially under 40-years-old, had slight but significantly higher activities than females. The levels were decreased in patients with gastric cancer. The levels were elevated in patients with hepatobiliary diseases, and had significant correlations with the results of the serum tests in hepatic diseases such as glutamic-oxaloacetic transaminase, glutamic-pyruvic transaminase, alkaline phosphatase and total bilirubin, but had no correlation with serum lactate dehydrogenase. In cellulose acetate electrophoresis, normal sera had a single peak at the beta-globulin region, but the sera in hepatitis or liver cirrhosis showed not only an increase in the normal peak at the beta-globulin region but also the appearance of the other one or two new peaks in the alpha1 and alpha2-globulin regions.
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PMID:Glycylprolyl beta-naphthylamidase activity in human serum. 114 81

We have recently utilized a prototype model of the Beckman Enzyme Activity Analyzer System-TR in our laboratory measuring various serum enzyme activities which include: alkaline phosphatase (ALP), E.C.3.1.3.1; creatine kinase (CK), E.C.2.7.3.2; hydroxybutyrate dehydrogenase (HBD), E.C.1.1.1.30; lactate dehydrogenase (LD), E.C.1.1.1.27; aspartate transaminase (AST), E.C.2.6.1.1; and alanine transaminase (ALT), E.C.2.6.1.2. Precision was found to be good. Sample activities could be measured as high as 1000 IU/1. The carryover studies fell within 2 SD of the means of the enzyme control studies. Coefficients of variation for ALP and CK were in the ranges of 0-40-2-14% and 0-52-4-30%, respectively. Correlation studies were done with GemSAEC and Gilford 300 N Spectrophotometer and the results were accurate, precise, and reproducible.
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PMID:Evaluation and utilization of a kinetic enzyme direct measuring photometer. 115 Aug 99

Methylglyoxal in doses over 25 mg/kg injected intravenously in cats and rabbits produces distinct changes in the cardiovascular and respiratory systems, but has no effect on respiration or circulation when injected intraperitoneally even in doses up to 1 g/kg. The effect of MG on blood pressure depends on the species of the animal. The effects of MG are dose-related and dependent on the route of its administration. Biochemical studies showed a significant rise in serum activities of creatine kinase (EC 2-7-3-2), lactate dehydrogenase (EC 1-1-1-27) and aspartate aminotransferase (EC 2-6-1-1-) after intraperitoneal injection of MG in the dose of 200 mg/kg in rabbits and 500 mg/kg in rats. The observed changes probably indicate damage of muscle tissue by MG, presumably as a result of low content of one of the glyoxalases in the muscles of the experimental animals. Elevation of glucose levels by MG was probably an adrenergic effect. These biochemical changes can serve to evaluate toxicity of MG preparations, which exhibit variations probably owing to varying degree of polymerization.
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PMID:Changes of certain pharmacological and biochemical indices in acute methylglyoxal poisoning. 116 55

The intra-subject correlations of three clinically meaningful combinations of serum constituents--(a) potassium, calcium, and albumin; (b) urea, creatinine, and uric acid; and (c) aspartate aminotransferase, lactate dehydrogenase, and alkaline phosphatase--were studied in 11 healthy men. Duplicate serum samples were obtained at 800 h, 1100 h, and 1400 h on five different days. All assays were performed on the AutoChemist Multichannel Analyzer. Correlation coefficients differed significantly among the subjects for the following six pairs of serum constituents: urea and creatinine, urea and uric acid, creatinine and uric acid, aspartate aminotransferase and lactate dehydrogenase, aspartate aminotransferase and alkaline phosphatase, and lactate dehydrogenase and alkaline phosphatase. Nonbiological positive correlation between analytical errors (i.e., errors of two different assays performed on the same specimen) was demonstrated for two of the pairs: potassium and calcium, and aspartate aminotransferase and lactate dehydrogenase. The error correlations of these two pairs of constituents comprised a significant component of the observed intra-subject correlations. Probable reasons for these analytical error correlations are discussed.
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PMID:Correlation of selected serum constituents: 1. Inter-individual variation and analytical error. 116 87


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