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)

Biotin deficiency in Aspergillus nidulans resulted in a 70% increase of the protein content and increased levels of free and bound aspartate, glutamate, serine, leucine and methionine. Likewise, the activities of NADP+ glutamate dehydrogenase, NAD+ gluatmate dehydrogenase, aspartate aminotransferase and alanine aminotransferase were significantly increased. The total RNA content increased while the DNA content was unaffected. The rRNA/tRNA ratio remained higher in biotin-deficient cells. Supplementation of glutamate, aspartate, serine, leucine and methionine to the culture medium raised the rRNA/tRNA ratio, and the difference observed in the qualitative and the quantitative patterns of protein and dry cell mass between normal and biotin-deficient cultures was abolished.
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PMID:Factors affecting protein synthesis during biotin deficiency in Aspergillus nidulans. 4 77

A prospective study of 181 patients suspected of having liver disease was carried out to determine the relative efficiencies of serum bilirubin (total and direct), alkaline phosphatase (AP), gamma glutamyl transferase (GGT), alanine aminotransferase (ALT), and aspartate aminotransferase (AST) with respect to diagnosis. Liver biopsies, liver scans, abdominal ultrasound, and clinical parameters were also tabulated and used independently to evaluate the patient's hepatic status and to determine the final diagnoses in each case. From the results of these tests for the 60 patients who were diagnosed as having liver disease, and the 87 patients who were felt to be free of liver disease, predictive values of the above tests were established. Data from this study suggests that while direct bilirubin is the most specific test, GGT is the most sensitive and has the fewest false negatives in the diagnosis of liver disease.
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PMID:Predictive values of various liver function tests with respect to the diagnosis of liver disease. 4 85

Antisera against rat liver aspartate aminotransferase (EC 2.6.1.1) isozymes were used to study the activity and immunologic pattern of these isozymes in the livers of the rat, mouse, hamster, gerbil and in Ehrlich ascites cells. A double immunodiffusion precipitin test and immunoelectrophoresis showed that, except for the gerbil, there was a pattern of identity of AAT isozymes in the presence of either the antianionic or the anticationic antisera. Although gerbil AAT isozymes are immunochemically different from those of the other rodents studied, they were inactivated by the respective antiserum in a manner similar to that observed with the other species. This may suggest that antigenic determinants at the catalytic site of each of the liver aspartate aminotransferase isozymes are least likely to change throughout the evolutionary process.
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PMID:Immunochemical pattern of aspartate aminotransferase isozumes in servral rodents and in Ehrlich ascites cells (38549). 4 35

Differentiation and calcification of cartilage of a fracture callus morphologically, ultrastructurally, and histochemically resembles cartilage of growing epiphyseal plate. The fracture callus includes the various cartilage cell types found in the epiphyseal plate. Proliferating and hypertrophic cartilage had higher activities of cytochrome oxidase, alkaline phosphatase and glutamate aspartate transaminase than fibrocartilage. Enzymes controlling glycogen synthesis and glycolysis had higher levels of activity in fibrocartilage than in hypertrophic cartilage. Lysosomal enzymes, catalase, 6-phospho-gluconic acid and glucose 6-phosphate dehydrogenase were uniformly distributed. Alkaline phosphatase was associated with extracellular vesicles found in hypertrophic cartilage. EM dense granules were found in mitochondria in hypertrophic cartilage. There was an increase of total lipids in hypertropic and calcified cartilage as compared to resting cartilage.
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PMID:Morphological and biochemical studies during differentiation and calcification of fracture callus cartilage. 4 43

In previous studies of rats with portacaval shunts, elevated gamma-globulin levels 2 weeks after shunt were attributed to antibodies to bacterial lipopolysaccharide, which were normally filtered by the liver. This study was designed to determine the tempo of this rise and the magnitude of hepatocellular damage within the first 4 days of the operation. Acute reversible hepatocellular damage was shown by elevated levels of aspartate aminotransferase which returned to normal within 48 hours. This was confirmed on histology. There was no rise in gamma-globulin during this study but levels of albumin were better maintained in shunted rats than in sham-operated rats. Levels of alpha2 and beta-globulin in the former fell in comparison with the latter animals.
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PMID:Acute biochemical and histological effects of portacaval shunt in the normal rat. 5 Jun 26

In experiments with albino rats it was found that after administration of phytobacteriomycin, trichotecin, hygromycin B or levoristatin into the stomach in doses of 1/20 of LD50 activity of the microsomal enzymes of the liver cells significantly changed and the changes persisted within at least 2 weeks. The above antibiotics induced similar changes in the lysosome enzyme, i.e. acid phosphatase, providing an increase in its activity. Changes in the activity of succinate dehydrogenase (mytochondria indicator enzyme), glucose-6-phosphatase (ribosome indicator enzyme) and aspartate aminotransferase (cytoplasm indicator enzyme) were different for each antibiotic. It is concluded that the above antibiotics were capable of impairing on intoxication the enzymatic function of various cell microstructures, though the levels of the change direction may be different.
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PMID:[Effect of phytobacteriomycin, trichotecin, hygromycin B and levoristatin on some rat liver enzymes]. 5 75

A five-step procedure is described for preparing highly purified aspartate aminotransferase (L-aspartate: 2-oxoglutarate aminotransferase, EC.2.6.1.1) from cell-freee enzyme extracts of Pediococcus cerevisiae. An overall purification of 130-fold was achieved. Some of P. cerevisiae aspartate aminotransferase properties were studied, i.s. pH optimum (7.8--8.0), optimum of temperature (37 degrees), Michaelis constans for 4 enzyme substrates and substrate specificity of enzyme. The enzyme is very thermolabile. During purification the enzyme was stabilizated by 2-oxoglutarate. The highly purified preparation was stored in the solution containing ammonium sulphate. The obtained aspartate aminotransferase preparation was free of alanine and aromatic amino acids aminotransferase activites and did not reveal malate dehydrogenase activity.
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PMID:Aspartate aminotransferase of Pediococcus cerevisiae. 6 56

Liver-function data were compared in 158 unselected hypertensives and 105 normotensives aged 45-64 years. Serum concentrations of alanine and aspartate aminotransferase (S.G.O.T. and S.G.P.T.) were higher, and more often raised, in the hypertensive patients. Serum bilirubin and alkaline phosphatase concentrations were similar in both groups. In hypertensive patients aminotransferase concentrations tended to be higher in those with increased alcohol intake.
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PMID:Alcohol and hypertension. 6 97

Mercurochrome strongly inhibits aspartate transaminase and 2,3-dicarboxyethylated aspartate transaminase. The native enzyme exhibits a biphasic time-course of inactivation by mercurochrome with second-order rate constants 1.62 x 10(4) M-1 - min-1 and 2.15 x 10(3) M-1 - min-1, whereas the modified enzyme is inactivated more slowly (second-order rate constant 6.1 x 10(2) M-1 - min-1) under the same conditions. The inhibitor inactivates native and modified enzyme in the absence as well as in the presence of substrates. Mercurochrome-transaminase interaction is accompanied by a red shift in the absorption maximum of the fluorochrome of about 10 nm. Difference spectra of the mercurochrome-enzyme system versus mercurochrome, compared with analogous spectra of mercurochrome-ethanol, revealed that the spectral shifts recorded during mercurochrome-transaminase interaction are similar to those that occur when mercurochrome is dissolved in non-polar solvents. Studies of mercurochrome complexes with native or modified transaminase, isolated by chromatography on Sephadex G-25, revealed that native transaminase is able to conjugate with four mercurochrome molecules per molecule, but the modified enzyme is able to conjugate with only two mercurochrome molecules per molecule.
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PMID:Interaction of aspartate aminotransferase with mercurochrome. Relationship of an exposed thiol group of the enzyme to the active centre. 7 75

A comparison of the cost of laboratory-made reagents with that of commercial kits was made for three serum-enzyme estimations and three serum-hormone estimations. The cost of reagents in kit form could only be justified on economic grounds for serum aspartate transaminase, alanine transaminase, and lactic dehydrogenase if the laboratory performed less than about 35 tests per day. It is unlikely that the use of kits for serum tri-iodothyronine, thyroxine, and thyrotrophic hormone can be justified on economic grounds for any workload. It is estimated that between 2 million pounds and 3 million pounds is spent unnecessarily by the National Health Service each year to purchase commercially prepared reagents for the six tests studied.
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PMID:Comparison of cost of preparing reagents in laboratory with cost of using commercial kits. 7 63


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