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)

1. The connection between feeding regime (food deprivation and restricted diet) and thermal acclimation (1-2, 6, 11 and 16 degrees C) was studied in rainbow trout held in diluted seawater (20% S). 2. At 1 degree C, food deprivation effects on all parameters are slight, and on RNA and certain enzymes they are masked by thermal acclimation effects. 3. At a salinity of 20% rainbow trout on a restricted diet and held at 11 degrees C have the highest growth rate. 4. Owing to increasing RNA levels, the RNA/DNA quotient is significantly higher than normal in rainbow trout held at 1 degree C although the fishes do not grow at this temperature. 5. Temperature and feeding both affect the enzymes we studied (liver: G1DH, AspT, arginase, G6PDH, and 6PGDH; kidney: G1DH, AspT, arginase, and Na/K-ATPase; white muscle: AspT and A1T; gill: Na/K-ATPase) differently. Interactions between these two factors also occur in some cases.
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PMID:Effects of temperature, food deprivation and salinity on growth, RNA/DNA ratio and certain enzyme activities in rainbow trout (Salmo gairdneri Richardson). 244 24

Plasma analysis for albumin, total bilirubin, and total protein values and aspartate aminotransferase (AST), arginase, and gamma-glutamyl transpeptidase (GGT) activities was used for the early and quantitative diagnosis of experimental Fasciola hepatica infections in beef calves. Calves were infected on 3 occasions with 1,000 (n = 5), 100 (n = 5), or 10 (n = 4) metacercariae for a total infective dose of 3,000, 300, or 30, respectively. Albendazole (15 mg/kg of body weight) was administered to 7 infected calves on postinfection (initial) week (PIW) 13. All calves were euthanatized and necropsied on PIW 16 for the determination of fluke infections. Plasma constituents were determined weekly. Significant (P less than 0.05) increases in AST activity occurred as early as PIW 4 and GGT activity at PIW 9, as compared with that in noninfected controls. Fluke burden-related differences were observed in GGT activity from PIW 9 onward. Increases in AST activity reflected parenchymal liver damage, whereas increases in GGT reflected hepatobiliary damage; therefore, differentiation could be made between the migratory and ductal phases of the infection. There was no correlation between arginase activity and fluke infection. As compared with fecal examination results, plasma enzyme analysis gave an earlier and semiquantitative indication of F hepatica infection in experimentally infected calves. Although increases in these plasma constituents were not definitely diagnostic of fascioliasis, useful information on the size of the fluke burden and progress of the disease process could be obtained by these methods. Plasma enzyme analyses of AST and GGT were not indicative of chemotherapeutic success or failure when calves with mature F hepatica (14 weeks old) infections were treated.
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PMID:Diagnosis of Fasciola hepatica infection in beef calves by plasma enzyme analysis. 286 Aug 32

This prospective study compared total plasma lipids, high-density lipoprotein cholesterol (HDL-C), and apolipoproteins A-I (apo A-I) and A-II (apo A-II) in 72 alcoholic patients and in 285 nonalcoholic controls. The HDL-C in the alcoholic group was not significantly different from that in the nonalcoholic controls. Alcoholic men had significantly higher levels of cholesterol and triglycerides and lower levels of apo A-I when compared with nonalcoholic controls. Alcoholic women had significantly higher levels of cholesterol and apo A-II when compared with nonalcoholic controls. Serial measurements in 25 alcoholic patients showed a significant decline in HDL-C, apo A-I, and apo A-II levels during the 4-wk hospital stay. HDL-C demonstrated its expected inverse relationship with plasma triglyceride level and its direct relationship with apo A-I, apo A-II, and the hepatic enzyme aspartate aminotransferase.
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PMID:Plasma lipids and apolipoprotein A-I and A-II levels in alcoholic patients. 396 5

The effect of variable doses of ethanol on plasma lecithin: cholesterol acyltransferase (LCAT) activity was examined in male, atherosclerosis-susceptible squirrel monkeys over a 12-month period. Primates were divided into three groups: 1) Controls fed isocaloric liquid diet; 2) Low Ethanol monkeys given liquid diet with vodka substituted isocalorically for carbohydrate at 12% of calories; and 3) High Ethanol animals fed diet plus vodka at 24% of calories. There were no significant differences between the treatments in serum glutamate oxaloacetate transaminase (SGOT), a measure of liver function. However, plasma LCAT activity (% esterification/min) measured in vitro was significantly reduced in High Ethanol monkeys while cholesterol esterification was elevated in the Low Ethanol group and intermediate in Controls. Similarly, the in vivo appearance of radiolabeled cholesteryl ester in high density lipoproteins (HDL) following the intravenous injection of 3H mevalonolactone was highest in the Low Ethanol primates, intermediate in Controls and significantly lower in monkeys fed the high alcohol diet. In vitro measurement of LCAT enzyme efficiency was similar for the three groups while substrate efficiency was lower in the High Ethanol treatment. Although LCAT activator (apoprotein A-I) was not markedly altered by dietary ethanol and the concentration of LCAT substrates (HDL free cholesterol and phosphatidyl choline) was significantly elevated in the High Ethanol group, subtle modifications in substrate-product composition may account for the observed reduction in cholesterol esterification. These include potential substrate and/or product LCAT inhibition resulting from increased concentrations of plasma free cholesterol, HDL lysophosphatidyl choline, and higher HDL2/HDL3 subfraction ratios, as well as alterations in HDL phospholipid fatty acid profiles in the High Ethanol group. Results from this study provide the first evidence of an anomalous enhancement in LCAT activity in nonhuman primates fed ethanol at 12% of calories and a marked depression in cholesterol esterification at the 24% dose which may be due to substrate alterations and product inhibition prior to overt biochemical evidence of liver dysfunction.
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PMID:Effect of ethanol on lecithin:cholesterol acyltransferase (LCAT) activity. 399 6

Two isozymes of aspartate aminotransferase have been demonstrated biochemically. One isozyme is found in the mitochondrial fraction of the cytoplasm, the other ("soluble") in the supernatant. Both isozymes can be demonstrated by the cytochemical technique of Lee and Torack, as reported in the preceding report. Aldehyde fixation rapidly inactivates both isozymes, especially the soluble one. Inactivation can be delayed by addition of ketoglutarate to the fixative. The ketoglutarate probably competes with the fixative for the active site of the enzyme, thus protecting that region of the molecule. This enables adequate tissue preservation with enough remaining enzymatic activity to be demonstrated by the precipitation of oxaloacetate as the lead salt from a medium containing alpha-ketoglutaric acid aspartic acid, and lead nitrate. Electron-opaque material was found not only in mitochondria but, as the result of substrate protection, on the plasma membranes of many cells including erythrocytes and bacteria, the limiting membrane of peroxisomes, and the transverse tubular system of striated muscle. Occasional centrioles, neurotubules, tubules in the tails of spermatozoa, the A-I band junction in myofibrils of striated muscle, and the ground substance between cisternae of endoplasmic reticulum in intestinal goblet cells also showed precipitate. In all cases, replacement of L-aspartic acid by D-aspartic acid in the medium resulted in unstained sections. The sensitivity of extramitochondrial sites to fixation, the need of ketoglutarate as an agent for protecting the enzymatic activity during the fixation process, and the known presence of only soluble isozyme in erythrocytes indicate that enzymatic activity at these sites can be attributed to the soluble isozyme. Localization of the soluble isozyme on the plasma membrane may be related to possible involvement in depolarization phenomena, amino acid transport, or synthesis of plasma membrane-bound mucopolysaccharides.
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PMID:The ultrastructural localization of the isozymes of aspartate aminotransferase in murine tissues. 553 35

Sixteen clinically normal, healthy ponies were randomly assigned to 4 groups and given aflatoxin B1 in doses of 0.045, 0.030, 0.015, and 0 (control) mg/kg of body weight per day for 21 days (or total doses of 0.945, 0.630, 0.315, and 0 mg/kg). The animals were allowed to recover for 3 months and then were reassigned to 4 treatment groups such that each group during the 2nd trial included a pony from each of the groups of the 1st trial. The animals in the new groups were intubated and were given aflatoxin in doses of 0.4, 0.2, 0.1, and 0 (control) mg/kg/day for 5 days ( or total doses of 2.0, 1.0, 0.5, and 0 mg/kg). Venous blood samples were drawn every other day to monitor for toxicosis; examinations were made for RBC and WBC counts, hemoglobin concentration, PCV, serum urea nitrogen, prothrombin time, and serum concentrations of aspartate aminotransferase, iditol dehydrogenase, alkaline phosphatase, albumin, gamma-glutamyl transferase, and arginase. There were no significant differences between treatment groups and controls (given no aflatoxin) in the toxicologic values examined for during the 1st trial. During the 2nd experiment, 2 of the ponies in the large-dose treatment gorup (2.0 mg/kg) demonstrated increased serum enzyme activities. These animals had been in the large-dose (0.945 mg/kg) and median-dose (0.63 mg/kg) groups during the 1st trial. Arginase, iditol dehydrogenase, and gamma-glutamyl transpeptidase activities became increased on the 4th day of treatment and continued to increase until the 6th day of the experiment (1 day after treatment was terminated). These enzymes approached control group values at 10 days after cessation of treatment. These increases were indicative of hepatocellular toxicity. It was concluded that the possibility of equine aflatoxicosis exists although ponies given high quality rations appear to be less susceptible than some other species. Prior exposure to aflatoxins may predispose to clinical toxicity on subsequent exposure, despite lack of expression of clinical signs.
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PMID:Effects of aflatoxins in young ponies. 612 12

Lactate dehydrogenase (LDH), succinate dehydrogenase (SDH), aspartate aminotransferase (AAT), glutamate dehydrogenase (GDH), AMP deaminase, ornithine transcarbamylase (OTC), arginase and glutamine synthetase (GS) activities were increased in the kidney of the rat during repeated ethanol loading. The significance of these findings is discussed.
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PMID:Renal ammonia metabolic response in the rat to repeated ethanol loading. 648 7

After prolonged application of ethanol the liver and brain of rats show an appreciable increase in lactate dehydrogenase activity, noticeable lowering of cytoplasmic aspartate and alanine aminotransferase activity, elevation of liver arginine succinate lyase activity with unchanged activities of other enzymes of the ornithine cycle (ornithine carbamoyltransferase and arginase), reduction of glutamate and malate dehydrogenase and mitochondrial aspartate aminotransferase activity in brain tissue. Concurrent application of ethanol and pyridoxine normalizes the effect of ethanol on liver arginine succinate lyase and on brain tissue lactate and malate dehydrogenase, mitochondrial and cytoplasmic aspartate aminotransferase and alanine aminotransferase.
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PMID:[Enzyme activity changes in chronic alcoholic intoxication and the simultaneous administration of pyridoxine]. 689 33

The effects of a high fat diet (30% (w/w) corn oil) on chronic streptozotocin-diabetic rats were investigated at the whole body level and at the enzyme level. The diet caused significant decreases in the extent of polydipsia (66% decrease), polyphagia (49%), polyuria (67%) and glycosuria (70%). The activities of selected hepatic enzymes from the glycolytic, gluconeogenic, ureogenic and lipogenic clusters were determined. The fat diet caused significant decreases (range: 47 to 54%) in the activity of the ureogenic enzymes carbamyl phosphate synthetase, ornithine transcarbamylase and arginase; had no effect on the glycolytic enzymes glucokinase, hexokinase and pyruvate kinase; partially decreased the diabetes-induced elevated activities of the gluconeogenic enzymes phosphoenolpyruvate carboxykinase (63% decrease), serine dehydratase (90%), alanine aminotransferase (31%) and aspartate aminotransferase (65%), and partially reversed the activity of one lipogenic enzyme, ATP citrate lyase.
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PMID:The effects of a high fat diet on chronic streptozotocin-diabetic rats. 692 68

Adult female dogs or pony mares were subjected to a nonlethal dose of CCl4 (0.5 ml/kg of body weight). Amounts of several plasma enzymes thought to be indicative of hepatic disease were monitored. Plasma enzymes alanine aminotransferase, aspartate aminotransferase (AST), alkaline phosphatase (ALP), arginase, gamma-glutamyltransferase (GGT), and iditol dehydrogenase (ID), as well as total plasma bilirubin, were determined in these animals before and after the administration of the CCl4. In the dog, GGT was not significantly increased, whereas ALP values were increased during days 1 to 6. In the pony, GGT was significantly increased during the entire course of the study, whereas ALP exhibited only small, transient (though significant) increases. Responses of ID, AST, and ALP were unremarkable when compared between the pony and the dog. Total bilirubin was significantly (P less than or equal to 0.05) increased from days 1 to 4 (pony) or days 5 to 8 (dog) after the CCl4 dose, but subsequently returned to or decreased below base-line values. Animals did not have evidence of icterus at any time. Seemingly, the dog and the pony are distinct clinical entities, and only the appropriate laboratory tests for each species should be used to provide information for the clinicopathologic evaluation of hepatic disease.
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PMID:Variations of plasma enzymes in the pony and the dog after carbon tetrachloride administration. 733 28


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