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 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

Gyrocotyle fimbriata isolated from the spiral valve of Hydrolagus colliei were washed, then held in a filtered seawater-penicillin-Tris buffer medium. Ammonia and urea release to the medium declined together and ammonia production was minimal when the urea concentration was below detectable limits. Alanine and smaller amounts of glycine were released to the medium at a more constant rate. After 12 hr the alanine-glycine excretion was more than 20 times the ammonia excretion. L-arginine, L-serine, L-histidine, and urea were most effective in stimulating ammonia production by whole worms; other L-amino acids were essentially ineffective. L-glutamate dehydrogenase, L-amino acid oxidase, uricase, and ornithine transcarbamylase were below detectable levels. L-serine dehydrase, L-arginase, L-histidase, and urease were detected in tissue homogenates and probably account for most of the endogenous ammonia production. L-arginase has a molecular weight of 28,000 by Sehpadex gel filtration. The high levels of glutamate-pyruvate transaminase and lower levels of glutamate-oxalacetate transaminase correlate with the high level of alanine excretion. It is concluded that (1) ammonia production is not strongly linked to the overall energy metabolism of Gyrocotyle and is probably a result of a series of unrelated enzymatic reactions such as the action of urease of urea from the tissue of the rat fish, and (2) alanine and glycine are the major nitrogen excretory products and their production is linked to the energy metabolism of Gyrocotyle.
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PMID:Ammonia formation and amino acid excretion by Gyrocotyle fimbriata (Cestoidea). 111 78

1. Rats were given moderate-selenium (4-5 mg/kg) or low-Se (0-5 mg/kg) diets during gestation and lactation. Their young were given diets with high (10 mg/kg), moderate or low Se contents from weaning, and groups of rats were killed at intervals during the 14-week experimental peroid. 2. Compared with young rats which received the low-Se diet, those which received the moderate- or high-Se diets had a high incidence of liver lesions and there were changes in liver Se content, haemoglobin concentration, packed cell volume, prothrombin activity, fibrinogen content, spleen weight, body water and serum glutamic-oxaloacetic and glutamic-pyruvic transaminas (L-aspartate : 2-oxoglutarate aminotransferase; EC 2.6.1.1 and L-alanine : 2-oxoglutarate aminotransferase; EC 2.6.1.2 respectively) and alkaline phosphatase (EC 3.1.3.1) activities. In those rats which received the high-Se diet the changes were more pronounced than in those which received the moderate-Se diet. 3. In young rats from dams given moderate-Se diets, which were themselves given the moderate-Se diet, the liver Se content decreased continuously, whereas rats given the same diet but from dams which had received the low-Se diet, the liver Se content increased continuously. There was a slight improvement of symptoms of Se toxicity in all groups by the 5th week of the experimental peroid. 4. The results suggest that there was an adaptation to chronic Se intake.
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PMID:Effects of ingestion of organic selenium in adapted and non-adapted rats. 112 69

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 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

L-Leucine-pyruvate transaminase obtained from Acetobacter suboxydans exhibited absorbance maxima to 280 and 332 nm. The 332 nm peak was derived from the coenzyme bound to the enzyme protein with the epsilon NH2 of a lysine residue. The transaminase showed reactivity against many L-amino acids. The relation between the reactivity and the structure of the amino donor is discussed. The Michaelis constants for L-leucine, pyruvate, L-alanine and alpha-ketoisocaproate were 6.7, 3.1, 7.1 and 0.9 mM, respectively. The equilibrium constant was 5.3. The activation energy at pH 5.0 was 8,800 cal/mol.
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PMID:Further characterization of L-leucine-pyruvate transaminase from Acetobacter suboxydans. 115 85

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

The distribution of alanine aminotransferase isozymes in several tissues from several species has been studied. In glycolytic tissues, such as skeletal and cardiac muscle, cytosolic alanine aminotransferase was the predominant form. In gluconeogenic tissues, such as liver and kidney, the concentration of the cytosolic alanine aminotransferase was much more variable; its presence, however, may be correlated with the presence of phosphoenolpyruvate carboxykinase in the same compartment. The particulate enzyme was found associated only with the matrix of the mitochondria. It was present only in those gluconeogenic tissues that can utilize alanine for glucose production, e.g. rat liver and pig liver and kidney; it was absent from rat kidney which cannot convert alanine to glucose. These observations, together with the kinetic parameters of the two isozymes, suggest that in vivo, mitochondrial alanine aminotransferase is involved in the conversion of alanine to pyruvate, while the cytosolic isoenzyme is mainly involved in the formation of alanine from pyruvate.
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PMID:Metabolic implications of the distribution of the alanine aminotransferase isoenzymes. 117 55

1. Bicarbonate stimulates the activity of rat brain cytoplasmic and mitochondrial alanine aminotransferase (EC 2.6.1.2) probably due to the enhanced affinity for its substrates. 2. Under the same conditions, the activity of crystalline aspartate aminotransferase was inhibited. 3. The role of bicarbonate buffer in regulation of alanine aminotransferase activity and synthesis of alanine are discussed.
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PMID:Effect of bicarbonate buffer on the activity of cytoplasmic and mitochondrial alanine aminotransferase. 117 9

Tests conducted with rats demonstrated that hydrocortisone and desoxycorticosterone-acetate (DOCA) manifest an effect close by its orientation with regard to mitochondrial and extramitochondrial forms of aspartate- and alanine-aminotransferase (ACT and ALT), as well as cytoplasmatic malate-dehydrogenase (MDG) of the liver. It was only mitochondrial MDG that lent itself to be inhibited by hydrocortisone, but it was induced by DOCA. Adrenalectomy resulted in inhibition on ALT and MDG and in activation of ACT and of mitochondrial LDG. A course-wise introduction of sulphapyridazine with an excess of deficiency of corticosteroids changed the effects of hydrocortisone with respect to cytoplasmatic LDG, as well as the effects of DOCA or adrenalectomy in regard to LDG and MDG.
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PMID:[Effect of corticosteroids on the enzymatic activity of hepatic tissue]. 118 92


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