Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.6.1.2 (alanine aminotransferase)
 26,722 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activity of enzymes of glycine and alanine synthesis (glutamate-pyruvate aminotransferase, aspartate-beta-decarboxylase, threonine aldolase, serine hydroxymethyltransferase, alanine-glyoxylate aminotransferase, aspartate aminotransferase) is studied in haemolymph, fat body, fibroin and sericine divisions of silk gland of silkworm Bombyx mori at terminal period of larva development. Alanine-glyoxylate aminotransferase activity in fibroin division of silk gland (34,6 mu mole of glycine/mg of protein/min-10(-3)), alanine aminotransferase--in sericine division (36,0 mu mole of alanine/mg of protein/min-10(-3)) aspartate aminotransferase 27,3 mu mole of glutamic acid/mg of protein/min-10(-3)) and alanine aminotransferase (35,8 mu mole of alanine/mg of protein/min-10(-3)) on fat body. The ratio of alanine-glyoxylate aminotransferase/glutamate-pyruvate aminotransferase activities in posterior division of silk gland is near to glycine/alanine ratio in silk fibroin. The character of the enzymes activity in silkworm tissues correlates with the silk formation rate.
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PMID:[Glycine and alanine synthesis enzymes in the tissues of the silkworm during its development]. 99 78

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

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

The effect of X-irradiation on the alanine- and aspartate aminotransferase activity in the liver, kidney and spleen of mouse. Acta Physiol. Pol. 1975, 26 (1): 95-101. The alanine- and aspartate aminotransferase (GOT and GPT) activities and the protein content were measured in the liver, kidney and spleen homogenates of mice exposed to a single whole body X-irradiation with a 900 r dose. The assays were performed in 6 h intervals during the first day and 24 h intervals from the 2nd until the 6th day after the exposure. Significant differences in the enzymatic activity were found in the course of 24 h in control animals and a marked increase of this activity was found after irradiation. This may be explained by changes in the permeability of the mitochondrial membrane for enzyme molecules.
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PMID:The effect of X-irradiation on the alanine--and aspartate aminotransferase activity in the liver, kidney and spleen of mouse. 113 Feb 24

The serum argino-succinate lyase (ASAL) activity was measured in preoperative and post-operative serum samples, from approximately 500 patients submitted to elective surgery. The results were compared with the determinations of 6 other enzyme activities on the same serum specimens. Serum ASAL elevations correlated highly with increases in serum alanine aminotransferase (ALT) activity, and were nearly twice as great. They also correlated well with serum aspartate aminotransferase (AST), but were approximately 2.7 times greater. It is confirmed that the serum ASAL activity is a sensitive and specific test for liver cell damage, suitable use in special conditions where high sensitivity is required.
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PMID:Serum arginino-succinate lyase: observations on the sensitivity and specificity of this test in the detection of minimal hepatocellular damage. 114 20

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

The activities of serum aspartate aminotransferase (EC 2.6.1.1, L-aspartate: 2-oxoglutartate aminotransferase, ASAT) and alanine aminotransferase (EC 2.6.1.2, L-alanine: 2-oxoglutarate aminotransferase, ALAT) were determined in the sera of 1484 apparently healthy subjects using kinetic methods according to the Scandinavian recommendation (33). In the adult sera the mean activity of ASAT was 21.4
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PMID:Activities of aspartate and alanine aminotransferases and alkaline phosphatase in sera of healthy subjects. 115 24

The activities of aspartate aminotransferase (GOT), alanine aminotransferase (GPT), alkaline phosphatase (alkP), creatine kinase (CPK), and ornithine carbamoyltransferase (OCT) were determined in liver, heart, skeletal muscle, brain, kidney, lung, spleen, adrenals, pancreas, thyroid, thymus, and red cells of 56 bovine fetuses varying in gestational age from 115 to 255 days. The tissue aminotransferase activities were the most variable with gestational age. The GPT activity of liver, kidney, spleen, and red cells and the GOT activity of red cells decreased with fetal age. The GPT activity of heart, brain, and skeletal muscle and the GOT activity of adrenal, brain, and skeletal muscle increased with fetal age. Increasing activities were also described for adrenal and brain alkP and for brain and skeletal muscle CPK. In contrast, the OCT activities were fairly constant for each tissue as a function of gestational age.
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PMID:Developmental changes of tissue enzyme patterns in the bovine fetus with gestational age. 116 76

1. In order to assess whether the potential ability of heart ventricular muscle and liver to metabolise substrates such as alanine, aspartate and lactate varies as the sheep matures and its nutrition changes, the activities of the following enzymes were determined in tissues of lambs obtained at varying intervals between 50 days after conception to 16 weeks after birth and in livers from adult pregnant ewes: lactate dehydrogenase (EC 1.1.1.27), alanine aminotransferase (EC 2.6.1.2), pyruvate kinase (EC 2.7.1.40), pyruvate carboxylase (EC 6.4.1.1), phosphoenolpyruvate carboxykinase (GTP)(EC 4.1.1.32), malate dehydrogenase (EC 1.1.1.37), aspartate aminotransferase (EC 2.6.1.1) and citrate (si)-synthase (EC 4.1.3.7). 2. In the heart a most marked increase in alanine aminotransferase activity was found throughout development. During this period the activities of citrate (si)-synthase, lactate dehydrogenase and pyruvate carboxylase also increased. There were no substantial changes in the activities of aspartate aminotransferase, malate dehydrogenase or pyruvate kinase. Pyruvate kinase activities were five times greater in the heart compared with those found in the liver. No significant activity of phosphoenolpyruvate carboxykinase (GTP) was detected in heart muscle. 3. In the liver the activities of both alanine aminotransferase and aspartate aminotransferase increased immediately following birth although the activity of alanine aminotransferase was lower in livers of pregnant ewes than in any of the lambs. As with alanine aminotransferase the highest activities of lactate dehydrogenase were found during the period of postnatal growth. No marked changes were observed in malate dehydrogenase or citrate (si)-synthase activities during development. A small decline in pyruvate kinase activity occurred whilst the activities of pyruvate carboxylase and phosphoenolpyruvate carboxykinase (GTP) tended to rise during development.
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PMID:Activities of enzymes concerned with pyruvate and oxaloacetate metabolism in the heart and liver of developing sheep. 117 28

Serum guanase, aspartate aminotransferase, alanine aminotransferase, creatine phosphokinase and hydroxybutyrate dehydrogenase activities were measured in 290 blood samples from 96 consecutive patients admitted to a Coronary Care Unit. Elevated serum guanase activities (greater than 2 U/l) were found in 19 patients (20%). The magnitude and frequency of these elevations did not negate the value of guanase as a "liver function test", since all cases with raised guanase also had abnormal serum alanine aminotransferase activities. This fact, together with other information in the literature, indicated that elevated serum guanase activity following myocardial infarction was consequent upon some degree of sub-clinical hepatic necrosis. Caution must be exercised when serum asparate aminotransferase is used as an index of heart muscle necrosis unless guanase or some other "liver specific" enzyme is known to be normal, or unless creatine phosphokinase or hydroxybutyrate dehydrogenase activities are elevated.
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PMID:Serum guanase activities after myocardial infarction. 117 93


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