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:2.6.1.2 (alanine aminotransferase)
26,722 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Tetrahymena pyriformis Wh 14 was grown in Erlenmeyer flasks under continuous stirring at 30 degrees C for three days . After the culture had produced dry matter of about 100 mg HCB was added in acetone at a dose level of 0, 0.001, 0.1 and 1.0 ppm to the culture and incubated for another 7 days. At a dose level of 0.001 ppm the activity of delta-aminolevulinate dehydratase, hexokinase, and pyruvate kinase remained unaffected but was increased for glutamic-oxaloacetic transaminase, glutamic dehydrogenase, isocitrate dehydrogenase, and malate dehydrogenase while 0.1 ppm HCB increased the activity of all enzymes studied, the only exception being glutamic-pyruvic transaminase, the activity of which was depressed by HCB exposure. A concentration of 1.0 ppm HCB depressed the activity of most of the enzymes below control values with the exception of the two mitochondrial enzymes, MDH and ICDH, studied here.
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PMID:Effect of hexachlorobenzene (HCB) on the activity of some enzymes from Tetrahymena pyriformis. 10 53

Regulation of the cytoplasmic enzymes, pyruvate kinase (PK), glucokinase (GK), phosphoenolpy ruvate carboxykinase (PEPCK), fructose-1,6-diphosphatase (FDP), ATP citrate-lyase (ATP-CL), NAD-malate dehydrogenase (NAD-MD), NADP-malate dehydrogenase (NADP-MD), glutamic-pyruvic transaminase (GPT), glucose-6-phosphate dehydrogenase (G6PD), and 6-phosphogluconate dehydrogenase (6PGD), in rat liver by dietary fat (F diet) and dietary sucrose (S diet) was investigated. Mealfeeding the S diet to adult rats for 5 and 9 months resulted in a diurnal dietary response (i.e., food response) variation of FDP, GK, ATP-CL, 6PGD, and PK, while meal-feeding the S diet to young rats resulted in diurnal dietary response variation of ATP-CL, G6PD, NADP-MD, 6PGD, GPT, and PK. Meal-feeding the fat diet results in essentially no diurnal variation in enzyme activity. The overall effect of meal-feeding, as compared with ad libitum feeding, of the S diet was to increase the levels of G6PD, ATP-CL, and NADP-MD and to decrease the level of PEck in the meal-fed rats. Young rats meal-fed the two diets have higher enzyme activities than meal-fed adult rats for the observed enzymes (except for GPT and NAD-MD). In general, hepatic levels of the enzymes studied are low in the F diet-fed animals and markedly higher for the S diet-fed animals. These results suggest that dietary carbohydrate specifically induces those enzymes involved in carbohydrate metabolism, whereas dietary fat does not affect their levels. On the basis of prior evidence for an early requirement of RNA synthesis for sucrose induction of G6PD, this widespread induction of liver enzymes by carbohydrate must indicate either increased synthesis of ribosomal RNA with later regulation of synthesis specifically of these enzymes or increased synthesis of a rather large group of specific messenger RNAs i.e., coordinate genetic control of a number of these enzyme messenger RNAs.
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PMID:Effect of dietary fat and sucrose on the activities of several rat hepatic enzymes and their diurnal response to a meal. 16 37

Correlation between pyruvate and lactate contents as well as between enzymes participating in turnover of the substrates (pyruvate- and lactate dehydrogenases, alanine aminotransferase, pyruvate kinase) were studied in rat liver tissue simultaneously with tumor growth and intensive thiaminotherapy. Thiamine, administered into rats carrying carcinosarcoma Woker-256 at a daily dose 12.5 mg/kg body weight, exhibited the normalizing effect on activity of enzymes studied, on quantitative content of LDH isoenzymes and on content of lactate in blood and of pyruvate in liver tissue. Possible effect of thiamine on pyruvate metabolism in tumoral impairment is discussed.
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PMID:[Thiamine and pyruvate metabolism in tumor-bearing rats]. 66 48

Cell-free extracts of Rickettsia typhi were tested for activities of enzymes of the tricarboxylic acid cycle, of glutamate catabolism, and of glycolysis. The organisms were grown in the yolk sacs of chicken embryos, harvested shortly before the time of embryo death, purified by Renografin density gradient centrifugation, and ruptured in a French pressure cell. The following enzymatic activities were demonstrated: high levels of malate dehydrogenase (MDH), moderate levels of glutamate-oxaloacetate transaminase, glutamate, succinate, and isocitrate dehydrogenases, and citrate synthase, and low levels of glutamate-pyruvate transaminase. The specific activities of some of these enzymes were higher when the rickettsiae were harvested at a time of active proliferation, 3 to 4 days prior to embryo death. Rickettsial MDH was differentiated from host MDH by its migration pattern on polyacrylamide gel electrophoresis. The activities of MDH and two other dehydrogenases, demonstrable after the cells had been disrupted, were absent from purified, intact rickettsial preparations. No activity was detected for glucose-6-phosphate, 6-phosphogluconate, glyceraldehyde-3-phosphate, lactate dehydrogenases, phosphoglucose isomerase, fructoaldolase, or pyruvate kinase. Our results suggest that extracts of R. typhi that contain demonstrable enzymes involved in the catabolism of glutamate and tricarboxylic acid cycle intermediates, unlike Coxiella burnetti, lack detectable glycolytic activity.
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PMID:Enzymatic activities of cell-free extracts of Rickettsia typhi. 82 Jun 44

In order to assess the extent to which metabolism within the sheep placenta may influence the transfer of metabolites between mother and foetus at different stages of gestation the activities of enzymes concerned with some aspects of carbohydrate, amino acid and keton body metabolism were determined in placental cotyledons resected from ewes during the last three months of pregnancy. The activities of pyruvate kinase (EC 2.7.1.40), lactate dehydrogenase (EC 1.1.1.27), malate dehydrogenase (EC 1.1.1.37), ATP citrate (pro-3S)-lyase (EC 4.1.3.8), citrate (si)-synthase (EC 4.1.3.7), acetyl-CoA synthetase (EC 6.2.1.1), acetyl-CoA acetyltransferase (EC 2.3.1.9) and 3-keto acid CoA-transferase (EC 2.8.3.5) per gram wet weight cotyledon do not change during the period studied. The activities of alanine aminotransferase (EC 2.6.1.2), aspartate aminotransferase (EC 2.6.1.1), isocitrate dehydrogenase (NADP+) (EC 1.1.1.42), ornithine-oxoacid aminotransferase (EC 2.6.1.13) and 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) show an increase in activity between the third and fourth months of pregnancy whilst the activities of arginase (EC 3.5.3.1) and possibly pyruvate carboxylase (EC 6.4.1.1) show an increase in activity between the fourth and final months of pregnancy. Ornithine decarboxylase (EC 4.1.1.17) activity declines to one tenth of its activity during this later period. The absence of detectable activities of phosphoenolpyruvate carboxykinase (EC 4.1.1.32) and ornithine carbamoyltransferase (EC 2.1.3.3) indicate that gluconeogenesis and urea synthesis from ammonia do not occur in the sheep placenta. It appears that the ability of the placenta to metabolise several substrates is achieved by the time the placenta reaches its maximum size at approximately 90 days.
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PMID:Enzyme activities in the sheep placenta during the last three months of pregnancy. 84 73

The rate of distribution of cell enzymes between the intravascular and extravascular space was studied, following a sudden decrease of enzyme activities in plasma. This rapid decrease of enzyme activities was achieved in rats by a rapid exchange of the blood with a twofold volume of a suspension of homologous erythrocytes in isoosmolar bovine serum albumin solution. After this plasmapheresis, the activities of seven cell enzymes in the plasma were decreased to 14 to 22% of their original values. The subsequent increase in activities showed different kinetics, depending on the enzyme. After 120 min, creatine kinase had reached the starting activity; malate dehydrogenase and aldolase reached their original activities after 180 min. Aspartate aminotransferase, glutamate dehydrogenase, alanine aminotransferase and pyruvate kinase increased more slowly and they had still not reached their starting values after 240 min. Repetition of the plasmapheresis after 90 min had no obvious effect on the kinetics of the subsequent activity increase. During the first minutes after plasmapheresis the adjustment of the activity equilibrium between the interstitial and the intravascular compartments depends mainly on the capillary permeability. It is therefore possible to determine half-life constants for the distribution of enzymes within the extracellular space. The constants for malate dehydrogenase and aldolase are almost identical with those determined by intravenous injection, whereas there are discrepancies in the constants for the remaining enzymes. The constants for pyruvate kinase and glutamate dehydrogenase are significantly lower, while those for aspartate aminotransferase, alanine aminotransferase and creatine kinase are significantly higher, than those determined after intravenous injection. Possible reasons for these differences are disucssed.
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PMID:[Plasmapheresis as an experimental model for studies on the extracellular distribution of enzymes. Distribution and transport of cell enzymes within the extracellular space. IV (author's transl)]. 93 47

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. 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

Biochemical method was adopted to examine 10 kinds of histologic enzyme spectrum activities in gastric intestinal metaplasia, carcinoma and normal or superficial gastritis mucosa taken from different sites from 17 fresh surgical specimens of stomach. The enzymes are aldolase (ALD), pyruvate kinase (PYK), phospho hexo-isomerase (PHI), lactic dehydrogenase (LDH), creatine phosphokinase (CPK), hydroxybutyrate dehydrogenase (HBD), glutamic-pyruvic transaminase (GPT), alkaline phosphatase (AKP), acid phosphatase (ACP), r-glutamyl-transpeptidase (gamma-GT). Among glycolytic enzymes the content of ALD, PYK in intestinal metaplasia were 24.5 u and 24.6 u respectively, which were higher than those in the normal mucosa (15.7, 18.0) and lower than carcinoma (28.4, 29.6) (P less than 0.01-0.05). The content of CPK in intestinal metaplasia was lower (218.5 u) than that in the normal (463.9 u) and higher than that in carcinoma (110.3 u) (P less than 0.01). Among protease and amino acid enzymes the content of HBD in intestinal metaplasia was lower (108.2 u) than those in the normal (221.3 u) and carcinoma (113.9 u) (P less than 0.05). The content of GPT in intestinal metaplasia was (6.7 u) which was lower than that in the normal (9.4 u) and higher than that in carcinoma (3.7 u) (P less than 0.01). The above results could provide reference indices for judging the potential malignancy of gastric intestinal metaplasia.
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PMID:[Relationship between gastric carcinoma and enzyme spectrum activity in gastric mucosal intestinal metaplasia]. 161 87

Several key enzymes related to carbohydrate metabolism were assayed in Setaria digitata. In the cytosolic fraction pyruvate kinase, phosphoenolpyruvate carboxykinase, malate dehydrogenase, malic enzyme, aspartate transaminase and alanine transaminase were found. Among the TCA cycle enzymes succinate dehydrogenase, fumarate reductase, fumarase (malate dehydration), malate dehydrogenase (malate oxidation and oxaloacetate reduction) and malic enzyme (malate decarboxylation) were detected in the mitochondrial fraction. Only reduced nicotinamide adenine dinucleotide (NADH) dehydrogenase, NADH oxidase and NADH-cytochrome c reductase were found in the mitochondrial fraction. The significance of these results with respect to the metabolic capabilities of the worm are discussed.
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PMID:Intermediary carbohydrate metabolism in the adult filarial worm Setaria digitata. 177 15


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