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 reaction of serine O-sulfate with cytosolic aspartate aminotransferase [John, R.A., & Fasella, P. (1969) Biochemistry 8, 4477] has been reinvestigated. As in the corresponding reaction with beta-chloroalanine [Morino, Y., Osman, A.M., & Okamoto, M. (1974) J. Biol. Chem. 249, 6684], the enzyme is inactivated over a 10-min period, and the absorption maximum at pH 5.4 shifts from 430 to 336 nm. Upon prolonged standing the peak shifts again over a period of 20 h to 455 nm, a behavior entirely similar to that reported by Morino et al. for beta-chloroalanine in the presence of 3 M formate. When the pH of either the 10-min product (1a) or the 20-h product (1b) is raised to 11 or above, a yellow, diffusible compound (2) is released from the protein. This compound as well as its dephosphorylation and reduction products has been isolated and studied by NMR spectroscopy. Compound 2 is identical with a compound formed from serine sulfate and glutamate decarboxylase by a similar reaction sequence [Likos, J.J., Ueno, H., Feldhaus, R.W., & Metzler, D.E. (1982) Biochemistry (preceding paper in this issue)] and is the product of an aldol condensation of pyruvate with pyridoxal phosphate. When the 20-h product 1b is reduced with sodium borohydride and then heated in a boiling water bath, a material identical with the reduction product of 2 is released. We propose that the 20-h product 1b consists of 2 bound to the enzyme. Pathways for the formation of the various compounds are proposed. These findings require a reevaluation of the mechanisms of action of many enzyme-activated inhibitors of pyridoxal phosphate dependent enzymes.
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PMID:Chemistry of the inactivation of cytosolic aspartate aminotransferase by serine O-sulfate. 681 25

Gentamicin sulfate at dosage levels of 10 and 20 mg/kg of body weight was administered twice daily IV to red-tailed hawks. Clinical signs, water consumption, and changes in blood chemical values were monitored. Tissues were examined grossly and ultrastructurally, using light and electron microscopy. Clinical signs of weakness and apnea were attributed to gentamicin-induced neuromuscular blockade in the 20-mg/kg group. Serum values of aspartate transaminase, alanine transaminase, cholesterol, inorganic phosphorus, total protein, albumin, and uric acid increased in some birds. There was a decrease in periodic acid-Schiff staining of proximal tubular brush borders. Increased numbers of cytoplasmic lysosomes, many of which contained myelin figures, in renal epithelial cells were seen at the ultrastructural level. All birds given 20 mg/kg died. Both dosage levels were considered toxic in red-tailed hawks.
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PMID:Toxicity of gentamicin in red-tailed hawks. 688 67

In 38 subjects, 24-h food-and-water deprivation during the Jewish fast day, Tisha b'Av, led to a 2.5-fold increase in plasma free fatty acids and to a doubling of the bilirubin concentration. There were also significant increases in serum sodium, chloride, total proteins, albumin, uric acid, phosphorus and alkaline phosphatase and aspartate aminotransferase activity. Serum glucose and triglycerides decreased in concentration. There were no changes in concentrations of urea, potassium, cholesterol or calcium. The marked increases in free fatty acids might constitute a hazard for those with impaired myocardial function.
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PMID:Effect of 24-hour food-and-water deprivation on biochemical variables in blood. 709 42

Two-week-old Diamond White poults were deprived of food, water, or food and water (food/water) for up to 3 days to estimate the effects of anorexia similar to that observed in parasitic infections. The weight loss of poults deprived of water for 48 hr was approximately the same as those deprived of feed. Loss of heart and pancreas weight was proportional to the loss of body weight, but moisture levels in the hearts of feed-deprived poults increased significantly by 24 hr. In contrast, moisture levels in the pancreas of poults in all three deprived groups decreased significantly by 24 hr; the pancreases were blanched and granular after 48 hr of feed deprivation. Packed red blood-cell volumes increased significantly by 48 hr in water- and feed/water-deprived poults and by 72 hr in the feed-deprived group. Plasma carotenoid and plasma aspartate aminotransferase (GOT) levels of deprived birds did not differ significantly from controls. Plasma total proteins were significantly decreased in feed-deprived poults by 72 hr, significantly increased in water-deprived poults, and unchanged in poults deprived of feed and/or water were not marked; therefore, even the severe anorexia sometimes associated with parasitic infections in turkeys probably would not appreciably effect the measurements of these parameters.
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PMID:Effect of feed and water deprivation on organ and blood characteristics of young turkeys. 710 65

1. The effects of implanting turkeys with trienbolone acetate (TA) upon fluid balance and blood chemistry were studied. 2. The Na and water contents of skeletal muscles were increased by TA treatment while K was unaltered. 3. The extracellular space expressed as a proportion of starved body weight was unaffected by TA implantation. 4. Plasma or serum concentrations of P, Ca, Mg, Na and K and activities of the enzymes aspartate aminotransferase [EG 2.61.1], creatine kinase [EC 2.7.3.2] and gamma-glutamyl transferase [EC 2.3.2.2] were not changed by TA treatment. 5. Packed cell volume was significantly increased by TA implantation after a delay of some 2 to 3 weeks while plasma protein concentrations were immediately decreased for a period of two weeks before nearly normal concentrations were obtained again. 6. Erythrocyte sedimentation rate was decreased by TA treatment, but serum protein electrophoretic pattern was unchanged.
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PMID:The effects of trienbolone acetate implantation of turkeys upon fluid balance and blood chemistry. 726 Jul 1

Exposure to simulated weightlessness (7-day water immersion and 7-day head-down tilt) caused a decrease in the activity of malate (MDH) and isocitrate dehydrogenase (ICDH), and creatine phosphokinase dehydrogenase (ICDH), and creatine phosphokinase (CPK) at the expense of its MM isoform whereas the activity of alanine (ALT) and aspartate aminotransferase (AST) and pattern of distribution of MDH isoforms remained unchanged. Exposure to acceleration of +3 Gz before and after simulated weightlessness revealed similar changes in the activity of MDH, ICDH, ALT, AST and MDH cytoplasmic fractions. However, the higher increase in the enzyme activity after simulated weightlessness may give evidence for a greater change in cell membrane permeability during acceleration effects that followed simulated weightlessness.
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PMID:[Energy-metabolism enzymes during combined exposure of the body to simulated weightlessness and gravitational overloads]. 728 61

Conditions were determined for rapid separation of cytosolic and mitochondrial compartments by digitonin fractionation of rat hepatocytes. The minimum time required for separation of mitochondrial and cytosolic enzyme markers decreased rapidly with increasing temperature. Kyro EOB, a non-ionic detergent, increases the release of cytosolic enzymes, particularly at lower temperatures. Experimental procedures are described for greater than 90% release of cytosolic enzymes and less than 2% release of mitochondrial enzymes in 3s. By using appropriate concentrations of digitonin and Kyro EOB in a fractionation medium maintained at 1 degrees C and a minimum time of exposure to the medium, nearly separate patterns of release were obtained for enzyme markers for the cytosol, mitochondrial matrix and mitochondrial intermembrane space. The distribution of enzymes that exist in more than one of these compartments was quantified by comparing their rates of release with those of marker enzymes. The cytosol/mitochondrial-matrix distributions for such enzymes in hepatocytes from starved rats were 16%/84% for aspartate aminotransferase, 34%/66% for fumarase and 77%/23% for ATP citrate lyase. In hepatocytes from rats that were induced to synthesize ATP citrate lyase by starvation and re-feeding, the ratio had increased to 95%/5%. The maximum cytosol/intermembrane-space ratio for adenylate kinase was 8%/92%. A procedure is also described for treating commercial digitonin that increases its solubility in water from about 1mg/ml to more than 800mg/ml.
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PMID:Subcellular distribution of enzymes determined by rapid digitonin fractionation of isolated hepatocytes. 737 59

The effects of HX solution and UW solution for rat liver preservation were studied with non-circulated isolated perfused rat liver model. Sixty-six inbred Wistar rat livers were randomly preserved for 12, 18, 24, and 30h with HX solution or UW solution. The effects were assessed by measuring hepatic tissue water content, sinusoidal lining cell mortality, Krebs-Henseleit's perfusate aspartate aminotransferase, the number of livers secreting bile during isolated perfusion, and by observing the morphological changes in liver. The experimental results suggest that the effects of HX solution for rat liver preservation be similar to those of UW solution within 24h storage.
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PMID:[The effective time of HX solution for rat liver preservation]. 749 20

The tolerance of chickens to monensin (12.5 mg/kg of feed) and maduramicin (3.0 mg/kg of feed) fed at a reduced dose in the presence of the antioxidant duokvin was studied in two experiments including 2 x 200 Tetra-82 broiler chickens. Tolerance was assessed by the appearance of clinical signs indicative of a toxic effect, the number of deaths, the groups' body weight gain, feed and drinking water intake, the aspartate aminotransferase (AST) and lactate dehydrogenase (LDH) activities, calcium ion, inorganic phosphate and total protein content of the blood plasma, the haematocrit value, and haemoglobin concentration. When applied at a dose that had proved to be optimum in the efficacy studies, neither the monensin-duokvin combination (12.5 mg monensin per kg of feed + 120 mg duokvin per kg of feed) nor the maduramicin-duokvin combination (3.0 mg maduramicin per kg of feed + 120 mg duokvin per kg of feed) exerted a statistically significant influence on the parameters tested.
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PMID:Toxicological studies on potentiated ionophores in chickens. I. Tolerance study. 749 72

Nitric oxide synthase produces NO, citrulline, water, and NADP at the expense of arginine, NADPH, and dioxygen. While citrulline has been considered to be an inert by-product of the high output inducible isoform of NO synthase (iNOS), we show here that immunostimulants induce a metabolic pathway in vascular smooth muscle cells, which enables them to regenerate arginine from citrulline. Regeneration of arginine from citrulline is accomplished by two urea cycle enzymes: arginino-succinate synthetase (AS) and argininosuccinate lyase (AL). Whereas AL is constitutive to vascular smooth muscle cells, AS mRNA and enzyme activity is markedly induced in cells by treatment with bacterial lipopolysaccharide (LPS). The induction of AS mRNA and activity by LPS follows a time course which mirrors that for iNOS but lags 1-2 h behind. As shown for iNOS, interferon-gamma does not itself induce AS but is synergistic with LPS. AS induction is suppressed by glucocorticoids, actinomycin D, and, to a lesser extent, cycloheximide. On the other hand, AS induction is unaffected by an excess of citrulline or the inhibitor of iNOS, N omega-methyl-L-arginine. Our results show the urea cycle enzymes AS and AL confer cells with the capacity to produce NO without a need for exogenous arginine. In conjunction with NOS, citric acid cycle enzymes that covert fumarate to oxaloacetate (fumarase and malate dehydrogenase) and oxaloacetate to aspartate (aspartate transaminase), AS and AL form a novel arginine-citrulline cycle that enables high output NO production by cells.
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PMID:Argininosuccinate synthetase mRNA and activity are induced by immunostimulants in vascular smooth muscle. Role in the regeneration or arginine for nitric oxide synthesis. 751 85


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