Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.6.1.2 (alanine aminotransferase)
 26,722 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The combined enzymological investigation including determination of the total activity of asparagine transaminase and alanine transaminase, two serum enzymes, alkaline phosphatase, gamma-glutamyl transpeptidase, acetyl cholinesterase, and butyryl cholinesterase was applied to two groups of pregnant women with pyelonephritis treated with ampicillin (12 patients) and roscillin (14 patients). The investigation was performed at the following stages: before the treatment, on the 7th and on the 12th day of the treatment. No statistically significant differences in the average values of the activity of the above enzymes at these stages were observed in patients of the both groups which indicated the absence of the hepatotoxic effect of the preparations on the patients of a group as a whole. An increase in the levels of transaminases recorded in some patients after discontinuation of the treatment course was evident of a possible cytotoxic effect of the drugs without the signs of cholestasis. The effect was connected with the initial functional renal insufficiency.
 ...
PMID:[Enzymological evaluation of the hepatotoxicity of ampicillin and its therapeutic form, roscillin, in the treatment of pyelonephritis in pregnancy]. 399 43

Toxic effects of thermo-oxidizing decomposition products of conveying belts made of PVC and rubber have been tested. The resultant smokes were passed through a protective absorber. During 14-days' post-exposure observation, an increased activity of asparagine, aminotransferase and in some animal alanine aminotransferase was found. Moderately increased pathomorphological changes were found in lungs (emphysema, oedema interstitial and bronchogenic inflammations), along with slight degenerative changes in the liver and kidneys. In the peripheral blood, increased amounts of erythrocytes and leukocytes were found.
 ...
PMID:[Toxic effect of volatile products of thermooxidizing decomposition of conveyor belts]. 406 90

Evidence is provided for the utilization of glutamine by calvaria and compact bone of rat. Glutamine was actively transported into calvaria, principally by sodium-dependent mechanisms; its uptake was significantly inhibited by neutral amino acids (alanine, proline, serine, asparagine) and glutamine analogs (L-glutamate-gamma-hydroxamate, albizziin). Glutamine was degraded to ammonia and glutamate by phosphate-dependent glutaminase, a mitochondrial enzyme present in both calvaria and compact bone. The enzyme exhibited an apparent Kmgln of 2.35 mM, a KactPO4 of 25 mM, and a broad pH optimum (7.5-9.5). It was inactivated by incubation of intact calvaria or bone homogenates with the glutamine analogs 6-diazo-5-oxo-L-norleucine (DON) and a 2-amino-4-oxo-5-chloropentanoic acid (chloroketone). Such treatment also severely inhibited (greater than 95%) both ammonia and 14CO2 formation from [U-14C]glutamine. Glutamate dehydrogenase, alanine aminotransferase, and aspartate aminotransferase activities were measured in bone. Amino-oxyacetate, an aminotransferase inhibitor, inhibited 14CO2 formation from [U-14C]glutamine. The data indicate that glutamine can serve as a precursor of ammonia, glutamate, other amino acids (alanine, aspartate, ornithine, proline) and carbon dioxide in bone and that phosphate-dependent glutaminase, transaminases, and citric acid cycle activity contribute to the observed metabolism.
 ...
PMID:Glutamine metabolism in bone. 613 80

The work presents the results of the correlation analysis and the regression equation between the number of T-lymphocytes, the levels of IgA, IgM, IgG and the dynamics of the fall of the alanine and asparagine transaminase levels; the work also presents the results of the leukocyte migration inhibition test and the data on the duration of the presence of asparagine transaminase and alanine transaminase in the blood. The relationship between the normalization of enzymatic samples from the liver and the immune status in patients with viral hepatitis A and B is shown.
 ...
PMID:[Immunological indices of viral hepatitis patients and the prognosis for the time periods of aspartate and alanine transaminase normalization]. 648 73

Workers exposed to naphtha, tungsten, vanadium, cobalt and titanium exhibited decreased activity of asparagine and alanine aminotransferase, cholinesterase and ceruloplasmin in blood serum, as compared to controls. Activity of lactic acid dehydrogenase was not changed significantly. It might be surmised that absorption of metals and naphtha exhibits inhibitory properties in relation to the enzymes determined.
 ...
PMID:[Effect of low concentrations of metals and benzin on serum enzyme activity]. 666 96

beta-Methylene-DL-aspartate, a new beta, gamma-unsaturated amino acid, is an irreversible inhibitor of soluble pig heart glutamate-aspartate transaminase (Ki approximately 3 mM with respect to the L-form; limiting rate constant for inactivation approximately 0.4 min-1). The new amino acid is the most specific inhibitor of glutamate-aspartate transaminase thus far studied. It does not inactivate pig heart glutamate-alanine transaminase, soluble rat kidney glutamine transaminase K, gamma-aminobutyrate transaminase (from Pseudomonas fluorescens), glutamate decarboxylase (Escherichia coli), snake venom L-amino acid oxidase, or hog kidney D-amino acid oxidase. In addition, the following enzymes were not inhibited by beta-methylene-DL-aspartate in rat tissue homogenates: gamma-aminobutyrate transaminase (brain), tyrosine transaminase (liver), glutamine transaminase L (liver), asparagine, transaminase (liver), ornithine transaminase (liver) or branch-chain transaminase(s) (kidney). Intraperitoneal injection of beta-methylene-DL-aspartate into mice decreased kidney and liver glutamate-aspartate transaminase activities but had no effect on liver glutamate-alanine transaminase activity.
 ...
PMID:Inhibition of glutamate-aspartate transaminase by beta-methylene-DL-aspartate. 683 Jun 31

In those chronically exposed to manganese the activity of alanine aminotransferase (ALAT), asparagine aminotransferase (AspAT), lactate dehydrogenase (LDH), cholinesterase (ChE) and ceruloplasmin (CPL) was determined. As compared with the control group, only enzymatic activity was statistically decreased. Thus, determination of the mentioned enzymes in blood serum is of little value for evaluation of an early stage of manganese toxic effects.
 ...
PMID:[Usefulness of various enzyme tests in the evaluation of the effects of chronic exposure to manganese and iron]. 688 56

We studied the effect of L-glutamine (Gln), the principal intestinal fuel, on proliferation of a porcine jejunal cell line, IPEC-J2. In cells synchronized by serum deprivation for 4 h, Gln stimulated ornithine decarboxylase (ODC; EC 4.1.1.17) in a dose- and time-dependent manner, with maximal effects at 10 mM in 3 h (P < 0.01). Similar effects were seen for the structurally related amino acid L-asparagine and serum. The Gln effect on ODC was specific, as isosmolar mannitol, glucose, methyl-beta-D-glucoside, L-phenylalanine, ammonia, and aminoisobutyric acid were ineffective. The alanine aminotransferase inhibitor aminooxyacetate (AO) inhibited the ODC stimulation by Gln in a dose-dependent manner (half-maximal inhibitory concentration = 0.5 mM). AO was not toxic to cells, as determined by propidium iodide uptake into nuclei. In addition, Gln stimulated a twofold increase of cellular 24-h [3H]thymidine incorporation above rates of control cells bathed in standard media (P < 0.01); this effect was also blocked by AO. Gln and phorbol 12-myristate 13-acetate stimulated ODC in a synergistic manner. The Na+/H+ exchange inhibitor methylisobutyl amiloride blocked the enhancement of ODC by Gln. Gln also induced the mRNA of the immediate-early gene c-jun. Gln stimulates proliferation in a porcine jejunal cell line through a mechanism requiring transamination and intact Na+/H+ exchange. This stimulation of enterocyte proliferation by Gln suggests that therapeutic Gln administration could facilitate epithelial recovery in the injured small intestine.
 ...
PMID:L-glutamine and L-asparagine stimulate ODC activity and proliferation in a porcine jejunal enterocyte line. 748 12

Alteration of the biochemical blood indices has been studied in patients with rheumatoid arthritis and lupus erythematosus that were treated with vaulen (V) and polysorb (P) enterosorbents. It was determined that alanine aminotransferase activity grew and albumin, urea, uric acid levels enhanced after the V treatment. Glucose level and alanine-, asparagine aminotransferases activities decreased after the P treatment. It is necessary to take into consideration these results when choosing an enterosorbent for treatment of patients with the immunocomplex rheumatic diseases accompanied by the liver parenchyma lesion and hyperuricemia.
 ...
PMID:[Changes of biochemical blood parameters under conditions of treatment with vaulen and polysorb enterosorbents]. 775 50

The capacity of the malate-aspartate shuttle was evaluated in periportal (PP-H) and perivenous subfraction of rat hepatocytes (PV-H). The rate of glutamine production from alanine was 34-fold higher in PV-H than in PP-H. Statistically significant differences between PP-H and PV-H were found for the activities of lactate dehydrogenase and pyruvate kinase but not for the activities of NAD(+)-malate dehydrogenase, aspartate aminotransferase, and mitochondrial alanine aminotransferase. The rate of glucose production from sorbitol and the rate of ethanol utilization were higher in PP-H than in PV-H. In the presence of phenazine methosulfate (PMS), the increments in these rates were significantly greater in PV-H than in PP-H. The capacity of malate-aspartate shuttle in the presence of alanine was significantly higher in PP-H than in PV-H but in the presence of asparagine was similar in PP-H and PV-H. The results suggest that the capacity of malate-aspartate shuttle distributes heterogeneously along liver lobules with the dominance in periportal zone and that the difference of the capacity may result from the difference in the transport of aspartate across the mitochondrial membrane.
 ...
PMID:The capacity of the malate-aspartate shuttle differs between periportal and perivenous hepatocytes from rats. 810 64


<< Previous 1 2 3 4 5 6 Next >>