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)

The toxicity of several halogenated and non-halogenated hydrocarbons (CH2Cl2, CHCl3, CCl4, C6H14, C8H10) in isolated rat hepatocytes were compared. Release of aspartate aminotransferase (AST) activity was rapid and concentration-dependent. Fractional AST release plateaued at 10-60 min following hydrocarbon exposure. Enzyme leakage at 60 min correlated with the oil/water partition coefficient (pi) of the compounds. All compounds, except n-hexane, also caused an immediate inhibition of the rate of cellular respiration. Inhibition of cell respiration also correlated with pi and was reversible. The recovery of cellular oxygen consumption was examined in detail for CCl4 and correlated with evaporation of the compound. These data suggest that acute hydrocarbon-induced injury in isolated hepatocytes is mediated by concentration-dependent direct solvent effects. Since halogenated hydrocarbons are widely used to induce general anesthesia, the clinical implications of possible direct effects by halocarbons on liver function in vivo and the potential relationship to liver injury are discussed.
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PMID:Rapid halogenated hydrocarbon toxicity in isolated hepatocytes is mediated by direct solvent effects. 362 14

The reaction of 3'-O-methylpyridoxal 5'-phosphate bound into the active site of aspartate aminotransferase with the substrate L-aspartate has been investigated. This methylated coenzyme is a very poor catalyst but it does function slowly to produce normal products of a transamination half-reaction. At pH 8.5 and above the characteristic absorption band of a quinonoid intermediate appears rapidly and becomes very intense when the aspartate concentration is raised to 2 M. At pH 6 the quinonoid band is not seen, but the conversion of the methylated coenzyme into 3'-O-methylpyridoxamine 5'-phosphate is about 7 times faster than at high pH with the pH dependence being determined by an apparent pKa of 8.1 at 30 degrees C. We suggest that the active site containing the methylated coenzyme carries a net charge 1 unit more positive than that of native enzyme. This causes a loss of some other proton from the active site and could leave the catalytic lysine-258 deprotonated in the quinonoid species. This may explain its inability to react rapidly. We have measured the spectral band shapes of the quinonoid species studied here and have compared it with that seen with native enzyme. Because of the close similarity we conclude that during normal transamination the proton bound to the imine nitrogen probably shifts onto the phenolic oxygen prior to or synchronously with the formation of the observed quinonoid species.
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PMID:Reactions of 3'-O-methylpyridoxal 5'-phosphate in aspartate aminotransferase. 366 81

To determine the cause of hepatic injury in patients with hypoxaemia, the persistence of liver susceptibility to toxic injury after hypoxia was investigated in rats. Centrilobular necrosis and marked elevation of serum glutamic-pyruvic transaminase (SGPT) and serum glutamic-oxaloacetic transaminase (SGOT) activities were induced by carbon tetrachloride (0.1 ml/kg body weight) given in the period between 3 h before and 21 h after exposure to 7% oxygen for 3 h. This observation, that a short period of hypoxia results in a prolonged sensitivity to carbon tetrachloride-induced liver injury, has not been described previously. The mechanism of the phenomenon is obscure. These observations suggest that the hepatic injury in patients with hypoxaemia may be caused not only by the hypoxia per se or chemicals administered before or during hypoxia, but also by chemicals given within 24 h of hypoxaemia.
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PMID:Potentiation of carbon tetrachloride hepatotoxicity by hypoxia. 380 2

The effect of halothane-induced hypotension on the development of postanesthetic myopathy was studied, using 6 healthy adult horses. Horses were anesthetized with halothane in oxygen for 3.5 hours on each of 2 occasions. Intermittent positive-pressure ventilation was used to maintain PaCO2 of 45 to 55 mm of Hg throughout both anesthetic exposures. By regulating the inspired halothane concentration, a mean arterial blood pressure of 85 to 95 mm of Hg (normotension) was maintained throughout the 1st anesthetic exposure, and a mean arterial blood pressure of 55 to 65 mm of Hg (hypotension) was maintained during the 2nd anesthetic exposure. All horses recovered uneventfully from normotensive anesthesia, but all had some muscle dysfunction after prolonged hypotensive anesthesia. Because of apparent animal discomfort and lameness involving more than 1 limb, 3 horses were euthanatized soon after they recovered from hypotensive anesthesia. The 3 other horses showed a degree of lameness. In addition, 1 horse had raised, swollen plaques over the hip, rib, and facial areas which were in contact with the surgical table, and another had evidence of facial nerve paralysis. One hour after the 6 horses stood after hypotensive anesthesia was completed, values obtained for aspartate transaminase and creatinine were significantly (P less than 0.05) greater than those obtained after normotensive anesthesia was completed. Aspartate transaminase, total bilirubin, and creatinine values were significantly (P less than 0.05) increased when compared with those obtained before horses were anesthetized. A large increase was measured in creatine kinase. Twenty-four hours after hypotensive anesthesia was completed, creatine kinase and lactate dehydrogenase in the 3 surviving horses were significantly (P less than 0.05) greater than those values after normotensive anesthesia was completed.
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PMID:Arterial hypotension and the development of postanesthetic myopathy in halothane-anesthetized horses. 382 55

Activities of the red cell enzymes hexokinase, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, lactic dehydrogenase and aspartate aminotransferase were measured in 17 chronic haemodialysis patients receiving androgen therapy, 15 untreated chronic haemodialysis patients and 15 normal subjects. Compared to normal subjects, untreated haemodialysis patients had similar reticulocyte counts but significantly increased levels of all five enzymes studied. This finding suggests the presence of a younger red cell population in the peripheral blood and is consistent with the shortened red cell survival known to occur in this clinical setting. Red cell enzyme activities in untreated haemodialysis patients were significantly correlated with one another and with the serum phosphate level. Moreover, in this population, red cell DPG content was directly related to hexokinase and glucose 6-phosphate dehydrogenase activities while haemoglobin-oxygen affinity (P50) was inversely related to all five enzyme activities. In contrast, in androgen-treated haemodialysis patients, despite higher reticulocyte counts, red cell enzyme activities were the same or lower than those in the untreated haemodialysis group and only slightly higher than those in normal subjects, suggesting an overall older red cell population. Moreover, relationships of red cell enzymes to one another, to serum phosphate levels and to both red cell DPG content and haemoglobin-oxygen affinity were significantly different in androgen-treated subjects than in the untreated haemodialysis group. These changes are consistent with a direct effect of androgens on red cell metabolism and an improved red cell survival during androgen therapy.
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PMID:Androgen therapy in haemodialysis patients. II. Effects on red cell metabolism. 382 30

Changes in three recognized liver function tests are reported following the use of propofol in 30 fit, unpremedicated women in whom propofol was used as the main anaesthetic agent. Doses of 140 to 330 mg were given, together with nitrous oxide and oxygen. All patients were undergoing minor gynaecological operations and all conformed to Grade 1 physical status of American Society of Anesthesiologists Classification. In none of these patients was there hypoxia or hypercarbia at any time during or following anaesthesia and none of the patients received any other drugs until completion of the study. No significant changes in liver enzymes (aspartate transaminase and alanine transaminase) or in serum alkaline phosphatase were detected.
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PMID:Changes in liver function tests after propofol ('Diprivan'). 387 86

Anaesthesia was induced in 24 horses with xylazine and ketamine and maintained with halothane (12 cases) or enflurane (12 cases) in oxygen. Pulse rate, arterial blood pressure, arterial blood gas values, respiratory rate and tidal volume were measured at regular intervals during anaesthesia. Serial venous blood samples were taken for assay of glucose, urea, haemoglobin, packed cell volume, gamma glutamyl transpeptidase, aspartate aminotransferase, alanine aminotransferase and creatine kinase. Operating conditions and the horses' behaviour in the recovery period were also recorded. In the case of the group of horses receiving enflurane, difficulty was experienced maintaining anaesthesia deep enough for surgery. This group also displayed greater respiratory depression. There were no significant differences between arterial blood pressure values, or any of the haematological or biochemical parameters recorded in each group. Recovery from anaesthesia was significantly faster in horses receiving enflurane but less smooth. It was concluded that, although enflurane appeared to be safe in the horse, the respiratory depression and the unpleasant recovery did not make it a desirable alternative to halothane.
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PMID:Clinical anaesthesia in the horse: comparison of enflurane and halothane. 397 74

The formation of pyridoxal and its phosphate from pyridoxamine phosphate by red cell haemolysates was measured in a centrifugal analyser by the formation of the fluorescent adduct with semicarbazide. Pyridoxal phosphate was found to react more rapidly than pyridoxal, thus permitting a distinction between the two products, and hence the measurement of phosphatase activity. Activity of the enzyme, pyridoxamine phosphate:oxygen oxidoreductase (deaminating) EC 1.4.3.5 (PPO) was measured in haemolysates from 72 Gambian women with evidence of riboflavin deficiency, and was repeated after 6 weeks of placebo or riboflavin supplementation. Those who received the riboflavin supplement responded with a marked increase in PPO activity, which was matched by a decrease in the activation coefficient (AC) of erythrocyte NAD(P)H2:glutathione oxidoreductase, EC 1.6.4.2 (glutathione reductase, EGR). No difference between the supplemented and unsupplemented groups was observed in the capacity of haemolysates to hydrolyse pyridoxal 5-phosphate, nor in the extent of activation of erythrocyte L-aspartate:2-oxoglutarate aminotransferase EC 2.6.1.1. by pyridoxal phosphate. Although the three subjects with low levels of D-glucose 6-phosphate: NADP 1-oxidoreductase EC 1.1.1.49 (G6P-D) had, as expected, correspondingly low AC's of EGR, their unsupplemented activities of PPO were in the same low range as those of the G6P-D-normal subjects, and they responded as G6P-D-normal subjects did to riboflavin supplementation. PPO thus does not appear to resemble EGR in retaining its flavin coenzyme during riboflavin depletion.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:A simple fluorimetric assay for pyridoxamine phosphate oxidase in erythrocyte haemolysates: effects of riboflavin supplementation and of glucose 6-phosphate dehydrogenase deficiency. 401 61

Dogs and white rats with experimental tetanus were examined for blood plasma lipids and red cells, their acid resistance, oxygen balance, cytochrome oxidase and aspartate transaminase activity and muscle ultrastructure. The amount of blood plasma lipids was found to be increased, the lipid content in red cells was lowered because of phospholipid washing out. The red cell resistance was lowered, their sedimentation rate was accelerated. Oxygen metabolism in muscles was first enhanced to form excess lipid peroxides, disturbing the integrity of cell membranes and myocyte ultrastructure, and then it was suppressed because of depletion of the compensatory mechanisms and eventuated in the destruction of part of cells and later on in the death of animals.
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PMID:[Changes in lipid metabolism, oxygen balance and muscle ultrastructure in tetanus in an experiment]. 407 63

1. A method is described for extracting separately mitochondrial and extramitochondrial enzymes from fat-cells prepared by collagenase digestion from rat epididymal fat-pads. The following distribution of enzymes has been observed (with the total activities of the enzymes as units/mg of fat-cell DNA at 25 degrees C given in parenthesis). Exclusively mitochondrial enzymes: glutamate dehydrogenase (1.8), NAD-isocitrate dehydrogenase (0.5), citrate synthase (5.2), pyruvate carboxylase (3.0); exclusively extramitochondrial enzymes: glucose 6-phosphate dehydrogenase (5.8), 6-phosphogluconate dehydrogenase (5.2), NADP-malate dehydrogenase (11.0), ATP-citrate lyase (5.1); enzymes present in both mitochondrial and extramitochondrial compartments: NADP-isocitrate dehydrogenase (3.7), NAD-malate dehydrogenase (330), aconitate hydratase (1.1), carnitine acetyltransferase (0.4), acetyl-CoA synthetase (1.0), aspartate aminotransferase (1.7), alanine aminotransferase (6.1). The mean DNA content of eight preparations of fat-cells was 109mug/g dry weight of cells. 2. Mitochondria showing respiratory control ratios of 3-6 with pyruvate, about 3 with succinate and P/O ratios of approaching 3 and 2 respectively have been isolated from fat-cells. From studies of rates of oxygen uptake and of swelling in iso-osmotic solutions of ammonium salts, it is concluded that fat-cell mitochondria are permeable to the monocarboxylic acids, pyruvate and acetate; that in the presence of phosphate they are permeable to malate and succinate and to a lesser extent oxaloacetate but not fumarate; and that in the presence of both malate and phosphate they are permeable to citrate, isocitrate and 2-oxoglutarate. In addition, isolated fat-cell mitochondria have been found to oxidize acetyl l-carnitine and, slowly, l-glycerol 3-phosphate. 3. It is concluded that the major means of transport of acetyl units into the cytoplasm for fatty acid synthesis is as citrate. Extensive transport as glutamate, 2-oxoglutarate and isocitrate, as acetate and as acetyl l-carnitine appears to be ruled out by the low activities of mitochondrial aconitate hydratase, mitochondrial acetyl-CoA hydrolyase and carnitine acetyltransferase respectively. Pathways whereby oxaloacetate generated in the cytoplasm during fatty acid synthesis by ATP-citrate lyase may be returned to mitochondria for further citrate synthesis are discussed. 4. It is also concluded that fat-cells contain pathways that will allow the excess of reducing power formed in the cytoplasm when adipose tissue is incubated in glucose and insulin to be transferred to mitochondria as l-glycerol 3-phosphate or malate. When adipose tissue is incubated in pyruvate alone, reducing power for fatty acid, l-glycerol 3-phosphate and lactate formation may be transferred to the cytoplasm as citrate and malate.
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PMID:The intracellular localization of enzymes in white-adipose-tissue fat-cells and permeability properties of fat-cell mitochondria. Transfer of acetyl units and reducing power between mitochondria and cytoplasm. 439 82


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