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)

The relationship between nitrogen assimilation, metabolism and aflatoxin formation has been investigated in a toxigenic and a non-toxigenic strain of Aspergillus parasiticus. Ammonia from the medium is mainly assimilated via NADP-requiring glutamate dehydrogenase. During growth NAD-requiring glutamate dehydrogenase followed an inverse pattern of activity with respect to NADP glutamate dehydrogenase. Alpha-ketoglutarate, the product of NAD glutamate dehydrogenase, stimulated acetate incorporation into aflatoxins. Glutamine synthetase, ornithine transcarbamylase, both utilizing glutamate as substrate were assayed under different growth conditions. An important regulatory role for glutamine synthetase is suggested. The metabolic route of asparagine utilization was also investigated. Both the known pathways, glutamate oxaloacetate transaminase and glutamate pyruvate transaminase are operative simultaneously.
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PMID:Nitrogen metabolism in Aspergillus parasiticus NRRL 3240 and A. flavus NRRL 3537 in relation to aflatoxin production. 287 96

The nucleotide sequence of ornithine aminotransferase mRNA from rat liver, including the entire coding and 3' untranslated regions, was determined from two overlapping cDNA clones. The mRNA encodes a precursor polypeptide of 439 amino acid residues with a molecular weight of 48,332. The deduced amino acid composition of the proposed mature enzyme sequence (residues 35 through 439) was in good agreement with that reported for the purified protein. The amino-terminal segment of the precursor corresponding to residues 1 through 34 has an overall positive charge, containing 6 basic residues and only a single acidic residue, and is postulated to be the mitochondrial leader sequence. The first 22 amino acid residues of the proposed leader sequences share 54% homology with the leader peptide of rat ornithine transcarbamylase precursor and more limited homology to the leader peptides of other nuclear-encoded mitochondrial matrix proteins. Homology was also observed between residues 286 through 362 ornithine aminotransferase precursor and a region containing the pyridoxyl phosphate binding domain of mitochondrial aspartate aminotransferase.
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PMID:Sequence of the precursor to rat ornithine aminotransferase deduced from a cDNA clone. 384 Apr 76

Previous observations that valproic acid (VPA) causes hepatic damage prompted us to investigate the effect of large doses of the drug (0.6, 1.2 and 1.8 mmol/kg/day) on a number of liver enzymes located on different subcellular fractions. In mitochondria, glutamate dehydrogenase, aspartate aminotransferase and ornithine carbamoyltransferase were significantly increased (1.8 mmol/kg/day). In microsomes, gamma-glutamyltransferase activity increased significantly (1.8 mmol/kg) and cytochrome P-450 content decreased significantly (1.2 and 1.8 mmol/kg). In cytosol, both aspartate and alanine aminotransferase activities were increased at all dose levels. These results indicate that VPA induces dose-dependent changes in some liver enzyme activities.
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PMID:Effect of sodium valproate on subcellular fraction enzymes in rat liver. 393 26

The electrophoretic separations of some human and pig liver enzymes on cellulose acetate and Cellogel were investigated, with reference to their joint occurrence in serum of patients undergoing treatment by extracorporeal pig liver perfusion. In every case it was possible to distinguish between the human and pig enzymes. Pig lactate dehydrogenase isoenzymes occupy a position slightly anodic to the corresponding human bands. The aspartate transaminase band of human is more anodic than that of pig, but their cathodic bands have the same mobility. Alanine transaminase of both human and pig liver extract is shown to exist as two bands each towards the anode. The faster moving human band is more anodic than the corresponding pig band, while the other human band is less anodic. Sorbitol dehydrogenase, alkaline phosphatase, and ornithine carbamoyltransferase all exist as one band each. Human sorbitol dehydrogenase is more cathodic than the pig enzyme, human alkaline phosphatase more anodic than the pig enzyme, while human ornithine carbamoyltransferase is less anodic than the pig enzyme.
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PMID:Electrophoretic separation and differentiation of enzymes from human and from porcine liver. 504 73

The activities of aspartate aminotransferase (AST), alanine aminotransferase (ALT), ornithine carbamoyltransferase (OCT), sorbitol dehydrogenase (SDH), gamma-glutamyl transferase (GGT), alkaline phosphatase (AP), lactate dehydrogenase (LDH) and creatine kinase (CK), were determined in eight organs of 10 healthy male blue foxes. OCT was absolutely liver specific and ALT was also found to be liver specific. SDH was also found primarily in the liver but its activity was relatively low. GGT was found almost exclusively in the kidneys. The highest levels of AP were observed in the kidneys and in the intestines. LDH together with AST was present in high activities in all the tissues tested. CK activity was highest in skeletal and cardiac muscles.
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PMID:Activities of some enzymes in the tissues of the blue fox (Alopex lagopus). 613 May 87

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

Differential diagnosis of acute viral hepatitis, persistent chronic hepatitis, aggressive chronic hepatitis, and post-necrotic cirrhosis can reasonably be achieved on the basis of three well-known liver-function tests: aspartate aminotransferase, alanine aminotransferase, and glutamate dehydrogenase. With use of principal-component analysis, these four liver diseases can be characterized by two criteria: a "cytolytic" criterion, correlated particularly with a membrane-permeability test--namely, alanine aminotransferase activity--and a "mitochondrial damage" criterion, which is associated with above-normal ornithine carbamyltransferase and glutamate dehydrogenase activities.
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PMID:Multivariate analysis of an enzymic profile for the differential diagnosis of viral hepatitis. 743 42

We developed a sensitive enzyme-linked immunosorbent assay (ELISA) for serum ornithine carbamoyltransferase (OCT) protein, and examined serum OCT concentrations in patients with various liver diseases. OCT concentrations were markedly elevated in cases of hepatic encephalopathy, 'acute on chronic', and those with the acute phase of acute hepatitis, moderately in chronic hepatitis, liver cirrhosis, hepatocellular carcinoma, primary biliary cirrhosis, and slightly in those with a fatty liver. High percentages (92-98%) of patients with chronic hepatitis, liver cirrhosis and hepatocellular carcinoma had higher than normal concentrations of serum OCT protein. There was a close correlation with aspartate aminotransferase (AST) and alanine aminotransferase (ALT) activities and moderate correlations with those of mitochondrial AST, glutamate dehydrogenase and gamma-glutamyltranspeptidase. The OCT/ALT ratio was higher in patients with liver cirrhosis than in those with chronic hepatitis (p < 0.001), and was still higher in cases of hepatocellular carcinoma (p < 0.05). In 2 patients with 'acute on chronic' disease, OCT concentrations decreased similarly with or more rapidly than AST or ALT activities after admission. In 2 patients with hepatic encephalopathy, the OCT concentrations changed similarly with AST and ALT activities. This OCT ELISA system will aid in diagnosing various liver diseases and in the follow-up of the patients, and the OCT/ALT ratio may serve for a differential diagnosis of liver diseases.
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PMID:Clinical evaluation of serum ornithine carbamoyltransferase by enzyme-linked immunosorbent assay in patients with liver diseases. 778 67


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