Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P17174 (aspartate aminotransferase)
 14,872 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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

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

A method is described in which the extent of myocardial infarction in man is assessed by mathematical analysis of the rise in plasma enzyme levels after infarction. Five enzymes are used in this study: lactate dehydrogenase (LDH); alpha-hydroxybutyrate dehydrogenase (alpha-HBDH); aspartate aminotransferase (GOT); creatine phosphokinase (CPK); and phosphohexoseisomerase (PHI). It is shown that a reasonable assessment of the total enzyme release, reflecting the extent of the infarcted area, can be made when a sufficient number of blood samples are taken after infarction. This could provide a method by which to judge therapeutic effects of intervention in the course of a myocardial infarction, as demonstrated in this study by the assessment of the effect of urokinase on the enzyme release after an infarct.
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PMID:Quantitation of infarct size in man by means of plasma enzyme levels. 119 41

Biochemical variables have been measured in a group of volunteers during and after a long-distance run. Plasma glucose levels remained relatively constant and a significant decrease in plasma bicarbonate was noted. Plasma sodium, chloride, total protein, albumin and calcium showed significant increased of an order compatible with water losses occurring during the run. Plasma potassium, urea, creatinine, uric acid, phosphate and bilirubin all show much more marked and variable increases. The plasma enzymes alkaline phosphatase, lactate dehydrogenase, aspartate aminotransferase and creatine kinase likewise increased significantly throughout the run. Whilst most constituents showed a tendency to return to normal at 20-30 hours after the run, gross increases were observed for aspartate aminotransferase and creatine kinase.
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PMID:The effect of long-distance running on some biochemical variables. 119 11

The following enzymes were determined in the serum and plasma of man, dog and rat: alanine aminotransferase, asparate aminotransferase, alkaline phosphatase, lactate dehydrogenase and alpha-hydroxybutyrate dehydrogenase. The enzyme assays were performed on an Eppendorf-Enzymautomat 5010 using optimised conditions at 25 degrees C. The enzyme-activities changed by variable amounts during standing of the blood. This concerned mainly lactate dehydrogenase, alpha-hydroxybutyrate dehydrogenase and aspartate aminotransferase in the serum of the rat. In human serum and in dog serum, and in the plasma of man, dog and rat this effect was only less pronounced.
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PMID:[Enzyme-activities in serum and plasma of man, dog and rat, and the variation of these enzyme activities during storage of the blood]. 121 61

In 47 patients treated at the Toxicological Clinic in Krakow for coal stove-gas poisoning, the aspartate aminotransferase, lactate dehydrogenase, LDH1 isoenzyme activities, and the lactate level were studied. Findings were compared with those of earlier investigations carried out on a group of patients poisoned by lighting gas; qualitatively changes in both groups were similar. The biochemical parameters studied aided in quantitative evaluation of the patients' condition: a threefold increase in lactate level on admission to the hospital and a likewise threefold increase in aspartate aminotransferase activity after 24 hrs of treatment are indications of severe poisoning.
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PMID:A comparison of two types of acute carbon monoxide poisoning. 124 99

Serum levels of lactate dehydrogenase, creatine kinase, and glutamate oxaloacetate transaminase show initial elevations within 12 hr of exposure to 2,000 rads of gamma-radiation to the thoracic region of rats. Significant decreases in heart muscle homogenate levels of these enzymes parallel initial elevations in the serum and may suggest that enhanced leakage of enzymes is a consequence of radiation injury to heart muscle. Insignificant alterations in mitochondrial glutamate oxaloacetate transaminase levels after exposure indicate that in vivo injury to the mitochondria from therapeutic levels of gamma-radiation is questionable. The results support the contention that ionizing radiation instigates alterations in the dynamic permeability of membranes, allowing leakage of biologically active material out of the injured cell.
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PMID:Radiation-induced enzyme efflux from rat heart: sedentary animals. 125 84

Intramuscular injections of digoxin, bumetanide, pentazocine or isotonic sodium chloride have been given to 39 patients. We followed the serum concentrations of creatine kinase (CK), aspartate aminotransferase (ASAT), lactate dehydrogenase (LDH) and LDH isoenzymes for 4 days. Ten patients receiving 500 mug digoxin showed a significant rise in CK, which lasted for 48 hours, and 6 of them had CK values exceeding the upper normal limit. Pentazocine in a dose of 30 mg given to 9 patients caused a significant rise in CK and LDH isoenzyme 1, but in no case did the level exceed the upper normal limit. No rise in ASAT or total LDH was found after digoxin and pentazocine injections. No changes in enzymes were discovered after bumetanide or isotonic sodium chloride. In the diagnostic evaluation of acute myocardial infarction, a moderate rise in CK must be assessed with caution when the patients have received i.m. injections of drugs with osmolarity and pH outside the physiological limits.
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PMID:The effect on serum enzymes of intramuscular injections of digoxin, bumetanide, pentazocine and isotonic sodium chloride. 126 67

Purified preparations of aspartate transaminase from pig heart cytosol contain a tightly bound proteolytic enzyme (approximately 2, 5%). The enzyme was separated from aspartate transaminase by gel-filtration on Sephadex G-100 in the presence of sodium dodecyl sulfate and by affinity chromatography on the column with Sepharose, containing covalently bound denaturated aspartate transaminase. Protease has a pH optimum of 9.0 and molecular weight of about 23.000-25.000. The proteolysis rates of different subforms of aspartate transaminase depend on their denaturation lability. A more stable choloenzyme is split at a slower rate than the apoenzyme. An enriched preparation of protease was also shown to split glutamate decarboxylase from E. coli and had no effect on cysteinlyase from hen egg, as well as on lactate dehydrogenase and albumin.
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PMID:[A proteolytic enzyme bound to the aspartate transaminase of swine heart cytosol]. 127 80


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