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)

Studies on aspartate aminotransferase (GOT) and L-alanine aminotransferase (GPT) of Paramphistomum explanatum have shown that GPT activity has more than twice the activity of GOT. The effect os some--SH reagents like cadmium, mercury, silver and iodoacetamide revealed that both enzymes were inhibited except that GOT was insensitive to cadmium ions. GPT was found to be much more sensitive to--SH reagents than GOT. There was unusual reaction to the two thiols used, cysteine and mercaptoethanol. Cysteine inhibited both the enzymes and mercaptoethanol activated GPT and inhibited GOT. Thiols in combination with iodoacetamide showed that the strong inhibitory effect of cysteine on both enzymes was reduced by iodoacetamide, but with mercaptoethanol the inhibitory effect on GOT was greater than when either of them was used alone, while GPT the effect of either counteracted each other. EDTA activated both enzymes and partially protected mercury inhibition of both enzymes and silver inhibition GOT only. It provided no protection against silver inhibition of GPT but complete protection of GPT against total inhibition by cadmium ions.
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PMID:Effect of some--SH and other reagents on aspartate aminotransferase and L-alanine aminotransferase of Paramphistomum explanatum Fischoeder, 1901. 41 89

Low turbidity, "clear" enzyme controls commercially produced in three concentrations and conventional human lyophilized control sera, which are more turbid, were evaluated to determine which was superior for quality control purposes. Criteria used to evaluate the controls were: 1) turbidity measurement, 2) daily assays for 30 days to estimate day-to-day precision, and 3) stability of the enzyme assay value for these controls when they were reconstituted and frozen for 0 to 30 days and 0 to 10 days with three aliquots separately prepared and frozen for 0 to 10 days for a total of 30 days. The controls were analyzed for lactate dehydrogenase, alanine aminotransferase, aspartate aminotransferase, creatine kinase, and alkaline phosphatase activities with the Perkin-Elmer KA 150 enzyme analyzer.
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PMID:The use of "clear" enzyme control materials. 42 91

The serum concentration of ethanol and the activities of aspartate aminotransferase, alanine aminotransferase and gamma-glutamyltransferase (GT) in 40 male chronic alcoholics were determined on admission to hospital. The serum activities of the enzymes were highest in patients with established alcoholism for less than 5 years. The serum concentration of ethanol, however, was lowest among these patients and gradually increased with the duration of alcoholism. No correlation was found between the serum ethanol level and the activity of any of the enzymes. The duration of the current debauch, which was shortest in cases of long-standing alcoholism, showed a positive correlation with the S-GT activity.
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PMID:Serum ethanol, hepatic enzymes and length of debauch in chronic alcoholics. 43 73

Normal values for 13 chemical constituents of plasma were estimated from results for 837 presumably healthy children. Ninety microliters of specimen was analyzed for lactate dehydrogenase, aspartate aminotransferase, alkaline phosphatase, inorganic phosphorus, total calcium, total cholesterol, total proteins, albumin, uric acid, urea nitrogen, alanine aminotransferase, total bilirubin, and glucose. We used two Abbott ABA-100 Bichromatic Analyzers interfaced directly to the ABA Data Management System. For each test age- and sex-related variations were assessed and normal values were estimated for six different age groups.
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PMID:Microchemical analysis for 13 constituents of plasma from healthy children. 43 35

Measurements of alanine aminotransferase and aspartate aminotransferase with the SMAC were evaluated for correlation with the ABA-100, precision, linearity, and carryover. We assayed 200 specimens with normal and abnormal aminotransferase activities with both the SMAC (y) and the ABA-100 (X). Linear regression analysis of the data yielded the following: alanine aminotransferase (r = 0.9732, y = 0.96x + 3.8); and aspartate aminotransferase (r = 0.9892, y = 0.90x + 2.1). Both aminotransferases demonstrated acceptable intra- and inter-assay variations with the SMAC and ABA-100. With the SMAC the upper limit of linearity for alanine aminotransferase was 350 U/L; that for asparate aminotransferase was 450 U/L. Carryover studies for SMAC indicate that specimens immediately following specimens with alanine aminotransferase activities greater 400 U/L and (or) aspartate aminotransferase activities greater than 500 U/L should be re-analyzed.
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PMID:Alanine aminotransferase and aspartate aminotransferase measurements with two automated analyzers, SMAC and the ABA-100, compared. 43 50

In order to verify the influence of sampling time on blood constituents, populations of supposedly healthy subjects were grouped according to age, sex, deviation from their ideal weight, state of fasting or nonfasting, and time of sampling. Each fasting subject in one group underwent two samplings during the course of a morning: the first at 08.00 and the second between 09.00 and 12.00. In the second group, the first was taken at 13.00, and the second between 14.00 and 16.00. Subjects in the second group had eaten a standard meal of 700 calories at 12.00. Differences between the paired samples from a given individual are discussed with respect to the time of sampling for plasma urea, creatinine, proteins, albumin, calcium, sodium, potassium, cholesterol, uric acid, chloride ions, phosphate, bilirubin, aspartate aminotransferase, alanine aminotransferase, lactate dehydrogenase, creatine phosphokinase, alkaline phosphatase, hemoglobin and erythrocyte and leukocyte counts. Variations due to the time of sampling were large for phosphorus, bilirubin, and leukocyte count.
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PMID:The effect of sex, deviation from ideal weight and sampling time on blood constituents in presumably healthy subjects. 43 75

We measured creatine kinase (EC 2.7.3.2) activity in 1009 serum samples from 538 patients in the intensive-care units of the University of Texas Medical Branch hospitals. Creatine kinase isoenzymes migrating cathodal to skeletal muscle creatine kinase (CK-MM) on cellulose acetate electrophoresis were found in sera from 14 of the 538 patients. Creatine kinase, lactate dehydrogenase (EC 1.1.1.27), aspartate aminotransferase (EC 2.6.1.1), and alanine aminotransferase (EC 2.6.1.2) activities were abnormally increased in these 14 patients. Liver lactate dehydrogenase isoenzyme (LDH5) and cardiac creatine kinase isoenzyme (CK-MB) were abnormally increased in 12 and eight of these patients, respectively. Ten of the 14 patients died during their hospital admission. We believe the creatine kinase isoenzymes that migrated cathodal to skeletal muscle creatine kinase (CK-MM) were of mitochondrial origin.
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PMID:Creatine kinase isoenzymes of mitochondrial origin in human serum. 44 29

In an experimental study, employing anaesthetized dogs, it was investigated whether cellular enzymes from peripheral skeletal muscle get into the circulating blood by diffusion across capillary membranes or by lymphatic transport. In the experimental group 1, the animals were anaesthetized only. The plasma activities of the four enzymes measured--lactate dehydrogenase, aspartate aminotransferase, alanine aminotransferase, creatine kinase--did not show any mentionable change during a time period of 6 h. In group 2 one hind limb of each animal was moved passively for 1 h. Alanine aminotransferase remained unchanged in plasma, the activities of the three other enzymes increased significantly. In group 3 one hind limb was made hypoxic by clamping the femoral blood vessels for 1 h. No activity changes were observed. When the period of hypoxia was followed by a 1-hour period of passive movement in group 4, the alterations in plasma activities were almost identical to those observed in group 2. In group 5 the experimental procedure was as in group 4, in addition the lymph from the thoracic duct was quantitatively withdrawn. The enzyme activities in plasma revealed a tendency to decrease rather than increase. Lymph flow increased significantly as well as the lymphatic activities of those enzymes which have high intracellular activities in muscle. The results prove, that enzymes from muscle are transported from the interstitial into the intravascular compartment mainly by lymphatic transport. Indications were found that the interruption of blood flow in one hind limb did not result in an enzyme release from muscle cells. It is discussed how changes in lymph flow, occurring during physical exercise for example, affect enzyme activities in plasma.
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PMID:Lymphatic transport of cellular enzymes from muscle into the intravascular compartment. 45 37

The administration of L-alpha-amino-beta-chloropropionic acid hydroxamide (L-ACPH) to mice brought about an inhibition in GABA-T activity in the brain of the animals, a significant inhibition occurring with dosage levels as low as 0.25 mmol/kg. Minimum levels of GABA-T activity were reached 3 h after administration of the drug. Brain glutamic acid decarboxylase, DOPA decarboxylase and aspartate aminotransferase activities were not altered by the L-ACPH but alanine aminotransferase activity was totally inhibited. Slight changes in structure caused great changes in the potency of the drugs. For example, the elongation of the L-ACPH structure by one carbon, or a change in the configuration of the amino group from L- to D-, caused a significant decrease in GABA inhibition. The chloro and hydroxamide groups were necessary for inhibitory activity. The administration of L-ACPH to mice delayed the onset of drug induced seizures but had a less noticeable effect against maximal electroshock. The addition of L-ACPH to crude extracts from brain, or to preparations of semipurified GABA-T, also inhibited GABA-T activity. Again the development of the inhibition was time-dependent. Possible mechanisms of action with respect to L-ACPH induced inhibition of GABA-T activity are discussed in the light of the data presented.
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PMID:Alteration of GABA metabolism in mammalian brain by l-alpha-amino-beta-chloropropionic acid hydroxamide and related compounds. 45 23

In rats, 3 days treatment with paracetamol (1 oral dose of 1 g/kg daily) produced a complete protection against the hepatotoxic actions of a further dose of paracetamol as documented by determination of serum enzyme activities (glutamic-oxaloacetic transaminase, (GOT), glutamic-pyruvic transaminase (GPT), sorbitol dehydrogenase (SDH), bromsulphthalein retention and histological investigations. Subacute paracetamol treatment decreased liver glutathione levels by 46%, liver microsomal cytochrome P-450 content by 23%, hepatic hydroxylation of aniline by 29% and hepatic demethylation of aminopyrine by 46%. It afforded also some protection against the hepatotoxic actions of carbon tetrachloride, bromobenzene and thioacetamide, but did not influence the antiphlogistic activity of paracetamol (carrageenan paw edema test). Plasma and liver concentrations of free paracetamol after oral administration of 1 g/kg paracetamol were somewhat higher in the subacutely paracetamol-pretreated rats than in the non-pretreated control animals whereas no differences in the concentrations of conjugated paracetamol were found between the 2 groups. Pretreatment with paracetamol did not influence the urinary excretion of free paracetamol but caused some shift in the urinary excretion of paracetamol conjugates: pretreated rats excreted 23% less of the paracetamol glucuronide and sulfate and 33% more of the paracetamol mercapturate than the control animals. A depression of the microsomal mixed-function oxidase activity is presumed to be the main cause of the paracetamol-induced protection against paracetamol hepatotoxicity.
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PMID:Studies on the mechanism of paracetamol-induced protection against paracetamol hepatotoxicity. 47 30


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