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)

1. Alkaline phosphatase [EC 3.1.3.1], acid phosphatase [EC 3.1.3.2], aspartate aminotransferase [ASAT, EC 2.6.1.1] and alanine aminotransferase [ALAT, EC 2.6.1.2] were measured in mucosal homogenates of different segments of the alimentary tract of White Rock cockerels. 2. The activities of acid and alkaline phosphatases were higher in the duodenum, jejenum and caecum than the anterior segments of the alimentary tract. 3. The activity of aspartate aminotransferase was higher in the oesophagus and crop than in the caudal segments of the alimentary tract. Alanine aminotransferase activity did not show any specific pattern. 4. The increased phosphatase activities in the caudal alimentary tract indicates their involvement in the nutrient transport across the mucosa. Aminotransferases were probably involved in the synthesis of amino acids and proteins in the anterior alimentary tract.
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PMID:Activities of acid and alkaline phosphatase and alanine and aspartate aminotransferase in different regions of the alimentary tract of adult White Rock cockerels. 322 95

Studies have been made on the activity of aspartate and alanine aminotransferase in the brain of 1, 4, 12-14, 16, 22 days, 1, 1 1/2, 3 months and 2 years old rats under hypothermic conditions (20-19 degrees C). It was shown that hypothermia decreases both total and specific activities of the enzymes in the developing brain. Alanine aminotransferase activity in brain homogenates determined at 37 and 20-19 degrees C, exhibits more significant changes than of aspartate aminotransferase.
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PMID:[Aminotransferase activity in the brain of rats of various ages during hypothermia]. 401 66

The electrophoretic separations of some human and pig liver enzymes on cellulose acetate and Cellogel were investigated, with reference to their joint occurrence in serum of patients undergoing treatment by extracorporeal pig liver perfusion. In every case it was possible to distinguish between the human and pig enzymes. Pig lactate dehydrogenase isoenzymes occupy a position slightly anodic to the corresponding human bands. The aspartate transaminase band of human is more anodic than that of pig, but their cathodic bands have the same mobility. Alanine transaminase of both human and pig liver extract is shown to exist as two bands each towards the anode. The faster moving human band is more anodic than the corresponding pig band, while the other human band is less anodic. Sorbitol dehydrogenase, alkaline phosphatase, and ornithine carbamoyltransferase all exist as one band each. Human sorbitol dehydrogenase is more cathodic than the pig enzyme, human alkaline phosphatase more anodic than the pig enzyme, while human ornithine carbamoyltransferase is less anodic than the pig enzyme.
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PMID:Electrophoretic separation and differentiation of enzymes from human and from porcine liver. 504 73

Rats were treated with 50 mg phenobarbital (PB) per kg body weight for 7 days prior to or after partial hepatectomy. The activities of aspartate aminotransferase, alanine aminotransferase, and glutamate dehydrogenase were measured in the regenerating liver 1 week following liver amputation. UDP-glucuronyl transferase activity was determined at the time of surgery as well as 7 days later at the time of death. Alanine aminotransferase was induced by PB in rats only treated in the postoperative period, while aspartate aminotransferase and glutamate dehydrogenase were not. The activity of UDP-glucuronyl transferase was increased more than twofold by repeated PB treatment in both normal and regenerating liver. After cessation of therapy, however, the enhanced activities returned to a normal level. It is concluded that UDP-glucuronyl transferase activity in regenerating liver is as inducible as in normal rat liver by repeated PB treatment despite incomplete hepatic regeneration. Preoperative PB treatment alone is not sufficient to stimulate the glucuronylating pathway in the late phase of liver regeneration.
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PMID:Late phase of liver restoration following partial hepatectomy in phenobarbital-treated rats. II. Effect of phenobarbital on aspartate aminotransferase, alanine aminotransferase, glutamate dehydrogenase, and UDP-glucuronyltransferase activity. 640 78

The activity of certain key enzymes involved in glutamic acid metabolism was studied in purified brain mitochondria and in mitochondrial subfractions separated in a discontinuous 1.2--1.6 mol/l sucrose gradient. Alanine aminotransferase and glutamate dehydrogenase were found to be matrix enzymes and aspartate aminotransferase to be associated with the inner mitochondrial membranes. After the purified mitochondria had been separated into 5 subfractions, aspartate aminotransferase and NAD+-dependent isocitrate dehydrogenase were found to be bound to the lighter mitochondrial subfractions settling at the 1.4--1.5 mol/l sucrose boundary while alanine aminotransferase, 4-aminobutyrate transaminase and glutamate dehydrogenase were associated with the heavier subfractions settling below 2.4 mol/l sucrose. The highest specific activity of the given enzymes was found in the subfraction settling at the 1.4--1.5 mol/l sucrose boundary, the only exception being alanine aminotransferase activity, whose maximum was found in the subfractions settling in 1.5 and 1.6 mol/l sucrose. It was concluded that alanine aminotransferase, in conjunction with glutamate dehydrogenase, is linked to NH3 binding and to the oxidation of reduced adenine nucleotides; in addition, alanine aminotransferase is presumed to have the function of transporting glutamate from the mitochondria to the extramitochondrial space.
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PMID:Alanine aminotransferase and some other enzymes in different populations of free brain cortex mitochondria. 645 52

It is demonstrated that plasma elimination constants for rapidly eliminated circulating tissue enzymes can be obtained from plasma time-activity curves if a slowly eliminated reference enzyme is simultaneously sampled. Enzyme and reference enzyme must be released together into the plasma. From the elimination constants thus obtained enzyme release into the plasma can be calculated as a function of time. The method can be applied during continuous release of enzyme into the plasma. The validity of the method is tested in the dog by intravascular infusion of a preparation of cytoplasmic enzymes, obtained by incubating dog liver under anoxic conditions. Alanine aminotransferase (ALT) was used as reference enzyme. Infused quantities of aspartate aminotransferase (AST), glucosephosphate isomerase (GPI) and ALT can be estimated with coefficients of variation (CV) of respectively 10, 19 and 7.6%. Application of the method to plasma time-activity curves of enzymes in patients after acute myocardial infarction (AMI), with alpha-hydroxybutyrate dehydrogenase (HBD) as reference enzyme, results in the following values for the fractional catabolic rate constants (FCR) of AST, GPI, creatine kinase (CK) and its isoenzyme CK(MB): FCRAST = 0.093 +/- 0.006 h-1; FCRGPI = 0.27 +/ 0.03 h-1 (mean +/- SE, n = 14); FCRCK = 0.20 +/) 0.02 h-1 (n = 30); FCRCK(MB) = 0.34 +/- 0.08 h-1 (n = 16). These values are considerably higher than mentioned by most authors, and this indicates that enzyme release after AMI has been underestimated. After AMI, enzymes are released in quantities proportional to the enzyme content of human heart tissue. Average release of CK conforms to this rule but large variations for individual patients are observed. Accurate estimates of the quantities of enzymes released into the plasma can be made for slowly eliminated enzymes by the use of fixed mean values for elimination constants. The results presented to this study indicate that tissue enzymes released from infarcted myocardium in patients after AMI are recovered quantitatively in the plasma. Local inactivation of enzymes or inactivation during the transport from heart to plasma is not significant in such patients.
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PMID:Quantitative analysis of plasma enzyme levels based upon simultaneous determination of different enzymes. 708 66

Tyrosine phenol-lyase from Erwinia herbicola was purified from a cell-free extract in a single step on Cibacron Blue F3GA-agarose. The protein was purified as the apoenzyme and was unstable after affinity chromatography. Alanine aminotransferase and aspartate aminotransferase from porcine heart also bound to Cibacron Blue F3GA-agarose. These enzymes were partially purified as holoenzymes from a crude porcine heart extract by elution with NADH and KCl. Alanine aminotransferase was purified 19 fold by this procedure.
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PMID:Affinity chromatography of some pyridoxal phosphate-requiring enzymes on Cibacron Blue F3GA-agarose. 725 63

The changes in both the levels of some free amino acids and their metabolism in the rat brain during the first 24 hr of postnatal life were studied. The content of glutamic acid decreased for the first 2 hr; it remained at the lowest level for the next 4 hr, when it began to increase. The content of alanine decreased for the first 6 hr and approached the adult level. Oxygen consumption, glucose oxidation, and pyruvate formation in the cerebral slices of the 24-hr-old rats were as much as 150% of that of the 19-day-old fetus. The distribution profile of radioactivity incorporated into the cerebral amino acids from the subarachnoid-injected [U-14C]glucose was also changed. In the 2- and 6-hr-old rats, 50% of the total radioactivity recovered in the free amino acids was in alanine. Its rate decreased to 30% in the 24-hr-old and was 2% in the adult, while the radioactivity incorporated into glutamic acid increased. Alanine aminotransferase activity started to increase at birth and had the highest level at 24 hr after birth. It then decreased and finally reached the same level as shown at birth. However, aspartate aminotransferase increased during the first 6 hr after birth and did not change until the end of the first day of life.
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PMID:Perinatal changes in amino acid metabolism of rat brain, especially alanine and glutamic acid. 746 80

Alanine aminotransferase (ALT) and aspartate aminotransferase (AST) of Echinococcus granulosus cyst wall harbored in mice for 10-12 months was measured. The activities of the 2 enzymes were 3,430 +/- 1,370-4,160 +/- 1,790 and 1,560 +/- 840-2,890 +/- 1,470, respectively. When infected mice were treated ig with mebendazole (Meb) 25 mg.kg-1.d-1 for 7-14 d, or 50 mg.kg-1.d-1 for 7 d, the ALT activities of cyst walls of both collapsed and full cysts were inhibited significantly with average inhibition rates of about 50%. Another benzimidazole derivative, albendazole (Alb), also inhibited ALT activity of the cyst wall with an inhibition rate of 40.7%, but this was not the case in the treatment with praziquantel 500 mg.kg-1.d-1 of the infected mice for 14 d. When the infected mice were treated ig with the above mentioned drugs at the same regimens, no apparent effect on AST activities of the cyst wall was seen except for the group treated ig with Meb at a higher daily dose, the inhibition rates being 26% (collapsed cyst) and 43.9% (full cyst). The significance of the results has been discussed briefly.
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PMID:Effects of mebendazole, albendazole and praziquantel on alanine aminotransferase and aspartate aminotransferase of Echinococcus granulosus cyst wall harbored in mice. 755 56

Two field studies were carried out in 1987 and 1991 in order to evaluate the effect of chronic exposure to solvent mixture on liver enzyme patterns. The results in 33 workers who participated in both studies and had complete sets of data are presented. The magnitude of chemical workload was assessed by means of ambient air monitoring and biomonitoring of solvent concentrations. Alanine aminotransferase, aspartate aminotransferase and gamma-glutamyl transpeptidase were used as markers for possible biological effects. No dose-response relationship was found between exposure to complex solvent mixtures in ambient air, reaching and sometimes even exceeding the threshold limit values for mixtures, and liver enzyme activities. Self-reported alcohol intake was the only factor identified as statistically related to increased liver enzyme activity.
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PMID:Hepatotoxic effects of solvent exposure around permissible limits and alcohol consumption in printers over a 4-year period. 781 94


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