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)

1. There was little difference in digestive (voluntary food intake, dry matter digestibility and nitrogen balance) and blood measurements (venous concentrations of corticosteroids, serum aspartate aminotransferase (EC 2.6.1.1), protein-bound iodine, urea and glucose) of intact sheep (eight animals) and of sheep prepared with rumen cannular (sixteen animals) and subsequently with either simple 'T-shaped' (eight animals) or re-entrant cannulas (eight animals) at the duodenum and ileum, when fed ad lib. a chopped medium-quality-hay ration. 2. Wool growth rates of the intact sheep were similar to those in sheep with rumen cannulas and with rumen cannulas plus simple 'T-shaped' cannulas, but higher (P less than 0-01) than those with rumen cannulas plus re-entrant cannulas. 3. When the sheep were subsequently given a restricted intake (800 g/d) of dried grass, retention times of solid- and liquid-phase digesta markers in the rumen and caecum were similar in all sheep. 4. The use of the different preparations in digestive physiology studies is discussed.
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PMID:The effects of various forms of gastrointestinal cannulation on digestive measurements in sheep. 88 73

Cerebrospinal fluid (CSF) samples were collected from the atlanto-occipital (AO) and lumbosacral (LS) subarachnoid spaces of 24 horses and 21 ponies that had no clinical evidence of neurologic disease. Depth of needle insertion, pressures, refractive index, rapid reagent strip test (protein, glucose, blood, pH) results, cell counts, content of protein, glucose, sodium, potassium, chloride, calcium, phosphorus, urea nitrogen, and cholesterol, and activities of creatine phosphokinase, aspartate transaminase, lactic dehydrogenase, and alkaline phosphatase were determined. The resulting clinical reference values obtained were discussed in light of the published normal values for CSF from horses, other animals, and man. White cell counts in CSF were found to be from 0 to 6/microliters. Values for protein content were distributed between wider limits than previously reported values. The LS-AO difference is proposed as a criterion for clinical evaluation of CSF protein content. Ponies were found to have more protein in their CSF than did the horses, and CSF from the LS site contained more glucose than that from the AO site. The CSF electrolyte composition was similar to that of previous reports. Enzyme activities in equine CSF are reported for the 1st time.
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PMID:Equine cerebrospinal fluid: reference values of normal horses. 91 Oct 95

We examined whether inter-individual differences in correlation coefficients previously found among subjects truly reflect consistent inter-individual differences or are time-related within an individual. The consitutents studied in this investigation were (a) the enzmes aspartate aminotransferase, alkaline phosphatase, and lactate dehydrogenase; and (b) the non=protein nitrogen-containing constituents urea, uric acid, and creatinine. Ten healthy women were each subjected to 15 venipunctures over a five-week period (Series I), and, after a two-month interval, were again subjected to 15 venipunctures over a second five-week period (Series II). Before statistical analysis, the data were corrected for the batch-to-batch (day-to-day) arnalytical variation. There was a signiificant (P less than .05) change in the covariance structure (variances or correlation coefficients, or both) between the two series in four of the 10 subjects for the combination of enzymes, and in three other subjects for the combination of nonprotein nitrogen constitutents. Although we found a significant (P lees than .05) average intra-individual variation in the mean values from series to series in the cases of the three enzymes and urea, the magnitude of the inter-series variation in means was relatively small. CV's were: alkaline phosphatase, 3.4%; lactate dehydrogenase, 2.3+; aspartate aminotransferase, 3.3%; urea, 5.0%; uric acid, 1.0%; and creatinine, 1.2%.
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PMID:Correlation of selected serum constitutents: 2. Consistency of intra-individual correlation values, means, and variances during four months. 97 46

A number of biochemical and haematological parameters, including plasma electrolytes, parameters of hepatic and renal function, plasma enzymes and free fatty acids were measured in 13 athletes before and after a 160-km 24-hour race. The runners were divided into 2 groups: group A, who competed the 160 km within 24 hours and group B, who either ran for 24 hours, or who retired before completing the distance. Minimal changes were found in the plasma electrolyte patterns in either group, whereas blood urea and creatinine levels increased during the race. The plasma enzymes increased to varying extents, the greatest increases being in lactic dehydrogenase, aspartate aminotransferase and the skeletal muscle specific MM isoenzyme of creatinine phosphokinase. Total bilirubin also increased, but no conclusive evidence of hepatic decompensation was found. Plasma free fatty acids levels were very markedly raised in 12 of the runners, the highest increases occurring in group A. All runners ingested carbohydrate during the race and this probably explains why the blood glucose levels increased slightly but remained within normal limits in all the athletes at the end of the race.
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PMID:Biochemical parameters in athletes before and after having run 160 kilometres. 98 11

Because of the difficulties in drawing blood for clinical chemistry in small laboratory animals there exist many methods for sampling blood and the preparation of serum, none of which is generally accepted or well standardised. It was the aim of this study to investigate the effects of sampling techniques on normal values of enzyme activities in the serum of rat and mouse. The activities of the following enzymes were determined: sorbitol dehydrogenase, lactate dehydrogenase, malate dehydrogenase, glutamate dehydrogenase, aspartate aminotransferase, alanine aminotransferase, pyruvate kinase, creatine kinase, myokinase, alkaline phosphatase and leucine aminopeptidase. In addition plasmaproteins, urea and inorganic phosphorus were measured. In rats blood was obtained from the following sites: retroorbital venous plexus, jugular vein, heart and ventral aorta. In mice blood was sampled from the jugular vein and the ventral aorta. Shifts of water from the interstitial to the intravascular space due to hypovolemia occurring during the experimental procedure were followed up by measuring the hematocrit and the distribution of radioiodide labelled albumin. In rats the activities of lactate dehydrogenase, malate dehydrogenase, aspartate aminotransferase, pyruvate kinase, creatine kinase and myokinase found in blood serum obtained from the retroorbital venous plexus and the ventral aorta were too high compared to the other sampling sites. Activities of alkaline phosphatase and alanine aminotransferase were slightly elevated when blood was sampled from the punctured retroorbital venous plexus. Small differences in plasmaproteins and hematocrit values were found to be due to acute shifts of water within the extracellular space. In mice the activities of lactate dehydrogenase, malate dehydrogenase, aspartate aminotransferase and myokinase were found to be too high in blood serum obtained from the ventral aorta. Efflux of enzymes from damaged cells and the interstitial space ive caused erroneous results too, but only to a minor extent. The most reliable method for blood sampling in rat and mouse is the cannulation of the jugular vein. The heart puncture can be recommended too. Attention should be paid, however, to the possibility of aspirating disrupted muscle cells through the inserted needle.
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PMID:[Effects of blood sampling on enzyme activities in the serum of small laboratory animals (author's transl)]. 108 84

Cytoplasmic aspartate aminotransferase from pig heart muscle was cleaved with cyanogen bromide and 8 peptide fragments were isolated. The high tendency of the large peptides for aggregation was overcome only by the utilization of special procedures of the denaturation and acylation of the lysine residues of peptide with citraconic anhydride. Peptides were separated by gel chromatography on sephadex G-50 and G-75 and by ion exchange chromatography on cellulose DE-22 and DE-32 with use of concentrated urea solutions. Amino acid composition and N-terminal residues of isolated peptides were determined.
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PMID:[Primary structure of the cytoplasmic aspartate aminotransferases from the swine myocardium. Isolation, purification and characteristics of the peptides from cyanogen bromide cleavage]. 113 91

The intra-subject correlations of three clinically meaningful combinations of serum constituents--(a) potassium, calcium, and albumin; (b) urea, creatinine, and uric acid; and (c) aspartate aminotransferase, lactate dehydrogenase, and alkaline phosphatase--were studied in 11 healthy men. Duplicate serum samples were obtained at 800 h, 1100 h, and 1400 h on five different days. All assays were performed on the AutoChemist Multichannel Analyzer. Correlation coefficients differed significantly among the subjects for the following six pairs of serum constituents: urea and creatinine, urea and uric acid, creatinine and uric acid, aspartate aminotransferase and lactate dehydrogenase, aspartate aminotransferase and alkaline phosphatase, and lactate dehydrogenase and alkaline phosphatase. Nonbiological positive correlation between analytical errors (i.e., errors of two different assays performed on the same specimen) was demonstrated for two of the pairs: potassium and calcium, and aspartate aminotransferase and lactate dehydrogenase. The error correlations of these two pairs of constituents comprised a significant component of the observed intra-subject correlations. Probable reasons for these analytical error correlations are discussed.
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PMID:Correlation of selected serum constituents: 1. Inter-individual variation and analytical error. 116 87

Biochemical variables have been measured in a group of volunteers during and after a long-distance run. Plasma glucose levels remained relatively constant and a significant decrease in plasma bicarbonate was noted. Plasma sodium, chloride, total protein, albumin and calcium showed significant increased of an order compatible with water losses occurring during the run. Plasma potassium, urea, creatinine, uric acid, phosphate and bilirubin all show much more marked and variable increases. The plasma enzymes alkaline phosphatase, lactate dehydrogenase, aspartate aminotransferase and creatine kinase likewise increased significantly throughout the run. Whilst most constituents showed a tendency to return to normal at 20-30 hours after the run, gross increases were observed for aspartate aminotransferase and creatine kinase.
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PMID:The effect of long-distance running on some biochemical variables. 119 11

Octanoate and L-palmitylcarnitine inhibited the synthesis of P-enolpyruvate from alpha-ketoglutarate and malate by isolated guinea pig liver mitochondria. A 50% reduction in P-enolpyruvate formation was obtained with 0.1 to 0.2 mM octanoate or with 0.06 to 0.10 mM L-palmitylcarnitine. At these concentrations, oxidative phosphorylation remained intact and only much higher concentrations of fatty acids altered this process. The addition of NH4Cl in the presence of malate and increasing concentrations of alpha-ketoglutarate (or vice versa) enhanced the formation of glutamate, aspartate, and P-enolpyruvate. The addition of increasing concentrations of NH4Cl in the presence of fixed amounts of malate and alpha-ketoglutarate had a similar effect. Furthermore, the inhibition of P-enolpyruvate synthesis by fatty acids and the reduction of the acetoacetate to beta-hydroxybutyrate ratio were reversed by the addition of NH4Cl. Cycloheximide, which blocks energy transfer at site 1 of the respiratory chain, decreased P-enolpyruvate formation. When cycloheximide and either octanoate or L-palmitylcarnitine were added together, there was an even greater reduction in P-enolpyruvate synthesis from either malate or alpha-ketoglutarate than was noted with either fatty acid alone. Since cycloheximide lowers the rate of ATP synthesis this may in turn reduce P-enolpyruvate formation by a mechanism independent of changes in the mitochondrial NAD+/NADH ratio caused by fatty acids. In the isolated perfused liver metabolizing lactate, the inhibitory effect of octanoate on gluconeogenesis was partially relieved by the addition of 1 mM NH4Cl, but remained unchanged in the presence of 2 mM NH4Cl, despite a highly oxidized NAD+/NADH ratio in the mitochondria. In contrast to glucose synthesis, urea formation was markedly increased during the infusion of 1 mM as well as 2 mM NH4Cl. After cessation of NH4Cl infusion, there was an increase in glucose production, to a rate as high as that observed in the absence of octanoate. This increase was accompanied by the disappearance of alanine, aspartate, and glutamate which had been stored in the liver during NH4Cl infusion. Urea synthesis also decreased progressively. These results indicate that gluconeogenesis in guinea pig liver is regulated, in part, by alterations in the mitochondrial oxidation-reduction state. However, the modulation of this effect by changing the concentrations of intermediates of the aspartate aminotransferase reaction indicates competition for oxalacetate between the aminotransferase reaction and P-enolpyruvate carboxykinase.
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PMID:Regulation of hepatic gluconeogenesis in the guinea pig by fatty acids and ammonia. 119 71

1. Isolated hepatocytes were used to establish the reasons for the accumulation of aspartate, previously observed when the isolated rat liver was perfused with ethanol in the presence of alanine or ammonium lactate. 2. The isolated cells did not form aspartate when incubated with alanine and ethanol, but much aspartate was formed on incubation with ammonium lactate and ethanol. 3. Urea was the main nitrogenous product on incubation with alanine, in contrast with the perfused liver, where major quantities of NH4+ are also formed. When the formation of urea was nullified by the addition of urease, alanine plus ethanol caused aspartate formation, indicating that aspartate formation depends on the presence of critical concentrations of NH4+. 4. The accumulated aspartate was present in the cytosol. Ethanol halved the content of 2-oxoglutarate in the cytosol and more than trebled that of glutamate in the mitochondria. 5. The findings support the assumption that 2-oxoglutarate formed by the mitochondrial aspartate aminotransferase is not translocated to the cytosol in the presence of ethanol and NH4+, because it is rapidly converted into glutamate, the dehydrogenation of ethanol providing the required NADH. Aspartate, however, is translocated to the cytosol and accumulates there because of the lack of stoicheiometric amounts of oxoglutarate.
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PMID:The accumulation of aspartate in the presence of ethanol in rat liver. 120 Oct 7


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