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)

Blood samples were taken for two successive years from canvasback ducks trapped in the Chesapeake Bay. The first winter (1972-1973) five plasma enzymes known to respond to organochlorine poisoning were examined. Abnormal enzyme elevations suggested that 20% of the population sampled (23/115 ducks) might contain organochlorine contaminants, but no residue analyses were performed. The second winter (1974) two of the same enzymes, aspartate aminotransferase and lactate dehydrogenase, and a third enzyme known to be specifically inhibited by lead, delta-aminolevulinic acid dehydratase, were assayed in 95 blood samples. Blood residues of organochlorine compounds and of lead were determined in representative samples, and the correlations between residue levels and enzyme changes were examined. The enzyme bioassays in 1974 indicated that lead was a more prevalent environmental contaminant than organochlorine compounds in canvasback ducks; 17% of the blood samples had less than one-half of the normal delta-aminole vulinic acid dehydratase activity, but only 11% exhibited abnormal aspartate aminotransferase or lactate dehydrogenase activities. These findings were confirmed by residue analyses that demonstrated lead concentrations four times higher than background levels, but only relatively low organochlorine concentrations. There was a highly significant inverse correlation between delta-aminolevulinic acid dehydratase activity and blood lead concentrations (P less than 0.01), and a weaker but significant correlation between plasma aspartate aminotransferase activity and blood PCB concentrations (P less than 0.05). It was apparent that delta-aminolevulinic acid dehydratase activity in the blood provided a sensitive and precise estimate of lead contamination in waterfowl. In canvasback ducks 200 ppb of lead in the blood caused a 75% decrease in delta aminolevulinic acid dehydratase activity, a magnitude of enzyme inhibition that disturbs heme synthesis and is regarded as detrimental in humans.
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PMID:Lead and PCB's in canvasback ducks: relationship between enzyme levels and residues in blood. 82 81

Of 101 consecutive hospitalised diabetic patients, 29 had elevated serum enzyme activities attributable to recognized clinical entities; 17% of the remainder had raised alkaline phosphatase (AP) activity, 15% had raised aspartate aminotransferase (GOT) activity, and 12% raised lactate dehydrogenase (LDH) activity in serum. Ketoacidosis and death within 3 months were commoner among patients with elevated serum enzyme activities than among those with normal enzymes. Study of 200 consecutive new untreated diabetics when first seen at an out-patient clinic revealed 15 with clinically explainable abnormal serum enzyme activities. Of the remainder, 11% had raised AP activity, 12% raised GOT activity, and 21% raised LDH activity in serum; these patients tended to have higher blood sugar concentrations than the subjects with normal serum enzymes. These abnormalities seem to be an intrinsic feature of diabetes mellitus which do not relate to duration, complications, or treatment of the disease. They do not seem to be directly related to hepatic involvement.
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PMID:Elevation of serum alkaline phosphatase activity and related enzymes in diabetes mellitus. 83 29

I evaluated the diagnostic value of routinely ordered liver-function tests in 175 biopsy-proven cases of hepatic disease by use of stepwise discriminant analysis. The tests studied-total and "direct" bilirubin, alkaline phosphatase, lactate dehydrogenase, and aspartate aminotransferase-correctly classified 45-73% of cases, depending on the homogeneity of the diagnostic groups. Aspartate aminotransferase and alkaline phosphatase were the best discriminators. When all tests were used in the most homogeneous groups (tumors, cirrhosis, and hepatitis), there was a stepwise improvement in diagnostic accuracy from 51 to 73%.
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PMID:Diagnostic effectiveness of biochemical liver-function tests, as evaluated by discriminant function analysis. 84 56

In order to assess the extent to which metabolism within the sheep placenta may influence the transfer of metabolites between mother and foetus at different stages of gestation the activities of enzymes concerned with some aspects of carbohydrate, amino acid and keton body metabolism were determined in placental cotyledons resected from ewes during the last three months of pregnancy. The activities of pyruvate kinase (EC 2.7.1.40), lactate dehydrogenase (EC 1.1.1.27), malate dehydrogenase (EC 1.1.1.37), ATP citrate (pro-3S)-lyase (EC 4.1.3.8), citrate (si)-synthase (EC 4.1.3.7), acetyl-CoA synthetase (EC 6.2.1.1), acetyl-CoA acetyltransferase (EC 2.3.1.9) and 3-keto acid CoA-transferase (EC 2.8.3.5) per gram wet weight cotyledon do not change during the period studied. The activities of alanine aminotransferase (EC 2.6.1.2), aspartate aminotransferase (EC 2.6.1.1), isocitrate dehydrogenase (NADP+) (EC 1.1.1.42), ornithine-oxoacid aminotransferase (EC 2.6.1.13) and 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) show an increase in activity between the third and fourth months of pregnancy whilst the activities of arginase (EC 3.5.3.1) and possibly pyruvate carboxylase (EC 6.4.1.1) show an increase in activity between the fourth and final months of pregnancy. Ornithine decarboxylase (EC 4.1.1.17) activity declines to one tenth of its activity during this later period. The absence of detectable activities of phosphoenolpyruvate carboxykinase (EC 4.1.1.32) and ornithine carbamoyltransferase (EC 2.1.3.3) indicate that gluconeogenesis and urea synthesis from ammonia do not occur in the sheep placenta. It appears that the ability of the placenta to metabolise several substrates is achieved by the time the placenta reaches its maximum size at approximately 90 days.
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PMID:Enzyme activities in the sheep placenta during the last three months of pregnancy. 84 73

The values of a number of biochemical variables have been studied before and after a 50-gram load of glucose orally. Reductions which were statistically significant were found for sodium, potassium, urea, total protein, albumin, calcium, phosphorus, urate, bilirubin, alkaline phosphatase, but not for bicarbonate, creatinine, creatine kinase, lactate dehydrogenase, aspartate aminotransferase, cholesterol, triglyceride or chloride. The magnitude of the changes was generally not great, but could be clinically appreciable. The differences may need to be taken into account in comparing population studies.
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PMID:The effect of 50 grams of glucose orally on a number of biochemical variables. 85 60

In a group of 113 consecutive patients taken into a coronary care unit on suspicion of acute myocardial infarction, blood samples were taken every 6 h and the following enzyme activities were measured: creatine kinase (S-CK), aspartate aminotransferase (S-ASAT), alanine aminotransferase (S-ALAT) and lactate dehydrogenase (S-LD). All measurements were made according to the Recommendations of the Scandinavian Committee on Enzymes. On all patients S-CK B subunit activity was determined by immunoinhibition with a specific anti CK M-subunit inhibitory antibody. At peak values of the respective total enzyme activities CK and LD isoenzymes were further qualitatively estimated by electrophoresis. The data indicate that even serial determinations of total CK, ASAT, ALAT and LD activities in serum do not provide the information required for a conclusive diagnosis of myocardial infarction in the individual case. In contrast, the positive predictive value (PV) of S-CK B was found to be 1.0 and the negative predictive value was 0.98. S-CK MB showed a PV pos. of 1.0 and also a PV neg. of 1.0. Electrophoretic determination of S-LD isoenzymes was slightly poorer with a PV pos. of 0.96 and PV neg. of 0.98. S-CK, total activity with nearly 9 per cent false positives had a positive predictive value of only 0.91, but a negative one of 1.0.
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PMID:Creatine kinase B-subunit activity in human serum. II. Evaluation of s-ck b-subunit activity in the diagnosis of acute myocardial infarction. 88 49

The electrophoretic mobility of several enzymes was studied in the embryos and early larvae of the hybrids between the loach (Misgurnus fossilis) and the aquarial cyprinids and cobitids (Acanthophthalmus). The cytosol aspartate aminotransferase is represented by one protein with the same mobility at all developmental stages both in the loach and in the hybrids. Malate dehydrogenase manifests four bands of isozymes which suffer no changes during the development. The electrophoretic profile of lactate dehydrogenase remains constant (10 isozymes) until hatching, but only 5 isozymes are found in the 5 days old larvae. Similar changes occur in the Misgurnus X Acanthophthalmus hybrids. The nonspecific esterases are represented by several proteins with different activities; their number increases after hatching. In the oocytes and adult specimens of Acanthophthalmus a characteristic and very active esterase was found which is absent in the loach. In the Misgurnus X Acanthophthalmus hybrids this esterase appears prior to the hatching and its activity later increases. Thus, the expression of the gene of one esterase begins in the end of embryogenesis.
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PMID:[Expression of genes controlling esterases during the embryonic development of hybrid fish]. 90 50

Serum creatine kinase, aspartate transaminase, and hydroxybutyrate dehydrogenase activities were abnormal in 76, 50, and 28% respectively of 50 patients studied within 26 hours of surgery. No patient showed clinical evidence of myocardial infarction. Creatine kinase MB isoenzyme elevation, and lactate dehydrogenase LD1 activity greater than LD2 (LD) greater than LD2) were infrequent (6 and 10% respectively). No patient showed the combination of transient MB isoenzyme elevation and LD1 greater than LD2, although their rare association without infarction after surgery is to be anticipated.
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PMID:Serum enzymes and isoenzymes after surgery. 92 Dec 11

The method for the determination of enzymic activity in turbid, lipaemic sera, which involves clearing by polyanion precipitation with heparin and magnesium chloride, was critically reviewed. In the diagnosis of diseases of the liver and pancreas, which are frequently associated with hyperlipoproteinaemia, only residual enzyme activities are measured in the cleared serum after polyanion treatment. In the measurement of glutamate dehydrogenase and in the Phadebas test for alpha-amylase, the enzymes are inactivated by treatment with heparin and magnesium chloride. On the other hand, as a result of polyanion precipitation gamma-glutamyl transferase is transferred, together with lipoproteins and chylomicrons, to the lipid-rich supernatant. Acid phosphatase also exhibits only residual activity in cleared serum. The activity of aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase, leucine arylamidase, cholinesterase, creatine kinase, lactate dehydrogenase, and alpha-hydroxybutyrate dehydrogenase, and the activity of alpha-amylase in the Merckotest are not affected by polyanion treatment of the serum.
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PMID:[Enzyme diagnosis in lipaemic sera before and after polyanion precipitation with heparin and magnesium chloride (author's transl)]. 92 35

Two new methods of activation were developed to graft enzymes on collegen films. They involved chemical modifications of surface groups of collagen either by Woodward's reagent "K" or by EDC, a water-soluble derivative of carbodiimide. EDC was a better coupling agent and a detailed study was conducted with this agent. It could be used either in a global method of activation and coupling, or in a two-step procedure of activation of collagen, followed by spontaneous coupling of enzyme. All enzymes tested were successfully bound: malate dehydrogenase, lactate dehydrogenase, aspartate aminotransferase, urease, creatine kinase, hexokinase. The influence on the yield of grafted enzyme, of pretreatment of films, time and temperature of EDC activation, concentration of EDC and enzyme, protecting agents was studied. Stability of enzyme activity on storage was greatly increased after grafting. A co-grafted dual system creatine kinase/heoxkinase, was achieved which exhibited a good efficiency. A striking renaturing process at 0-4degreesC after thermal denaturation, was observed with hexokinase.
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PMID:Grafting of enzymes on collagen films using Woodward's reagent "K" and a water-soluble carbodiimide derivative. 95 53


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