Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.6.1.2 (alanine aminotransferase)
 26,722 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The present study was designed to test if both the intensity and duration of the 45-min Square-Wave Endurance Exercise Test (SWEET) would produce changes in serum enzyme activities. Nine men, four sedentary (S) and five athletes (A), performed VO2 max and SWEET, at their Maximal Intensity of Endurance (MIE45) as defined by maximal heart rate and the impossibility of maintaining MIE 45 + 5% for 45 min. Arterial blood was sampled at rest (R), exercise (Ex) (45th min) and during recovery (15th min) for measurements of levels of Haemoglobin (Hb), Haematocrit (Hct), pH and seven serum enzymes: Creatine kinase (CPK), Hexose-phosphate isomerase (PHI), Aldolase (ALD), Lactate dehydrogenase (LDH), Malate dehydrogenase (MDH), Aspartate amino-transferase (ASAT or GOT), and Alanine aminotransferase (ALAT or GPT). Five enzymes increased significantly during exercise (MIE45), the delta % (Ex - R/R) increases were as follows: PHI (72%), MDH (28%), LDH (21%), CPK (17%), and GOT (13.5%), whilst only a 10% increase was observed for Hct and Hb and there was no significant change in the arterial pH. There was no correlation between the delta % of Hb, Hct, pH, and the results for the enzymes. Thus, it does not seem that haemoconcentration and arterial blood acidosis which occur during exercise are only at the origin of the observed increases in enzymes. A difference between "sedentary" and "athletes" subjects was found at rest and exercise (delta % = A - S/S) for CPK (R = 222%; Ex = 235%), GOT (R = 90%; Ex = 75%) and ALD (R = 99%; Ex = 54%). These results suggest that the MIE45, by measured increases in enzymatic activity, seems to require great muscular effort.
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PMID:Serum enzyme variations in men during an exhaustive "square-wave" endurance exercise test. 653 38

Statistical analysis of variance was applied to data from determinations of 14 plasma constituents in 25 rats in order to evaluate the analytical, experimental and biological (inter-and intraindividual) component of variance. Blood was taken seven times in intervals of 8-10 days, the last one by catheter technique and the other by heart puncture. The analytical portion of variance was determined by the concurrent analysis of a pool plasma standard. The experimental component of variance was evaluated by the comparison of the variation of the catheter values with that of the pooled data from heart puncture. The coefficient of variation for the latter may be grouped into three categories: less than 10% for protein, Na+, K+, Ca2+; 10-20% for urea, phosphate and the enzymes as alanine aminotransferase, choline esterase, alkaline phosphatase and leucine arylamidase and 20-65% for the other enzymes lactate dehydrogenase, malate dehydrogenase, aspartate aminotransferase and creatine kinase. The results from the samples taken by catheter technique generally revealed the lower values for the mean as well as for the variance. It became evident that the procedure of heart puncture is afflicted with the most aggravating interference factors, thus accounting for most of the experimental component of variance. The observed differences between the single blood drawings, the non-Gaussian distribution for several constituents, and the interactions between the components of variance do not always fit for the statistical concept of additivity of the single components.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Biological, analytical and experimental components of variance in a long-term study of plasma constituents in rat. 660 70

Seeking to determine the effect of liver disease associated with Reye's syndrome on the regulation of plasma pyridoxal 5'-phosphate, we measured this compound in plasma from 11 patients with biopsy-proven Reye's syndrome. Its concentrations in plasma are significantly higher [37.5 (SD 6.13) micrograms/L] at the onset of the disease than after treatment [8.50 (SD 2.9) micrograms/L] or in a group of hospitalized patients with no evidence of liver disease [8.4 (SD 1.5) micrograms/L]. The concentration of pyridoxal 5'-phosphate in plasma at the time the patients entered the hospital correlated significantly with their activities of serum alanine aminotransferase.
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PMID:Abnormal regulation of pyridoxal 5'-phosphate in Reye's syndrome. 661 34

The relationship between pyridoxal phosphate deficiency and activities of serum and liver aminotransferases was studied in 12 patients with alcoholic hepatitis. Plasma pyridoxal phosphate and the activities of liver aminotransferases were initially decreased in the patients, as compared with mean values in controls with normal hepatic histology. Addition of pyridoxal phosphate to liver homogenates increased liver alanine aminotransferase, but not aspartate aminotransferase, in all patients with initially low plasma pyridoxal phosphate. After 1 mo of abstinence from alcohol, with intake of an adequate diet and pyridoxine supplementation, plasma pyridoxal phosphate increased in all patients with initially low values (p less than 0.02). Serum aspartate aminotransferase decreased, whereas serum alanine aminotransferase increased, resulting in a decrease in their ratio in serum (p less than 0.001). Liver alanine aminotransferase increased (p less than 0.005), whereas liver aspartate aminotransferase remained unchanged. These data suggest that pyridoxal 5'-phosphate depletion is partially responsible for the low serum alanine to aspartate aminotransferase ratio that is typical of patients with alcoholic hepatitis.
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PMID:Relationship between pyridoxal 5'-phosphate deficiency and aminotransferase levels in alcoholic hepatitis. 669 65

The single intravenous administration of T-2 toxin to calves (0.25 mg/kg body weight) caused a marked decrease in the total peripheral white cell count which correlated with a decline in the neutrophil count. The circulating lymphocyte and platelet counts were unaffected by the toxin. A decline of approximately 10% occurred in hematocrit following toxin administration. A small transient increase was observed in serum aspartate aminotransferase, and lactate dehydrogenase activity together with a transient increase in the BSP retention test. There was no consistent pattern in the alteration of serum alanine aminotransferase activity and serum alkaline phosphate activity was unaffected by the toxin. The results suggest that in cattle the liver may not be the primary target organ for the cytotoxin effects of T-2 toxin.
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PMID:Effect of T-2 toxin on bovine hematological and serum enzyme parameters. 670 98

The addition of pyridoxal-5-phosphate for assay of alanine aminotransferase has been recommended. The referral methods are inconvenient for high volume instrumentation due to use of multiple reagents and blanks. We adapted a well-documented method to the centrifugal analyzer as a reference for adaptation of two kit methods. Reference intervals obtained and linearity determined were all similar. The kit methods compared favorably to the referral method. Linear regression analysis yielded the following: DOW = 1.011 BERG + 1.666, r = 0.9965; SKI = 0.938 BERG + 4.559, r = 0.9926; and DSKI = 1.028 BERG + 1.051, r = 0.9889. Precision of the assays was acceptable. We concluded that automation of reagent kits incorporating pyridoxal-5-phosphate is feasible and the assays compared favorably to a recommended method. High volume instrumentation can be used without denigration of analytical quality and to allow comparability to a documented method for interlaboratory review.
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PMID:Comparison of pyridoxal phosphate-supplemented reagent kits for alanine aminotransferase using centrifugal analysis. 673 98

The possibility that the glycosomes present in the bloodstream form of Trypanosoma brucei [Opperdoes, F. R. and Borst, P. (1977) FEBS Lett. 80, 360--364] constitute a separate pool of glycolytic intermediates within the cell was investigated. In titrations of intact cells with digitonin, a differential activation of glycolytic enzymes was observed. Enolase, pyruvate kinase and the cell-sap marker alanine aminotransferase were activated at 0.05 mg digitonin per mg protein. The nine glycosomal enzymes involved in the conversion of glucose and glycerol into 3-phosphoglycerate were activated only at digitonin concentrations between 0.7 and 9.8 mg/mg protein. In subcellular fractions the activities of the latter enzymes were all latent between 70 and 92%. Latency was abolished by addition of 0.1% Triton X-100 or partly by five cycles of freezing and thawing. We conclude that the glycosomal enzymes are surrounded by a membrane, which forms a permeability barrier to intermediates and co-factors of glycolysis. The concentrations of glycolytic intermediates and of adenine nucleotides were measured under aerobic conditions as well as in the presence of 1 mM salicylhydroxamic acid, a respiratory inhibitor. Addition of salicylhydroxamic acid caused the following changes: (a) The levels of almost all glycolytic intermediates measured decreased. Glycerol-3-phosphate, however, increased fourfold. (b) The phosphate potential was drastically lowered from 2900 to 450 M-1. (c) The trypanosomes became more reduced, as monitored by a change in the apparent redox state of the NADH/NAD+ courple from E'h = -189 to E'h = -219 mV. From the high levels of metabolite concentrations found and from comparison of the apparent mass-action ratios calculated for the separate glycolytic reactions with those for other organisms, we conclude that in bloodstream form T. brucei the glycolytic intermediates are present in the glycosomes as well as in the cytosol and that the two pools of intermediates equilibrate with each other, despite the presence of the glycosomal membrane.
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PMID:Glycolysis in Trypanosoma brucei. 676 64

beta-Alanine aminotransferase from rabbit liver has been purified 1,700-fold over the initial liver extract. The purified enzyme was shown to be homogeneous by disc electrophoresis and SDS polyacrylamide electrophoresis. The molecular weight of the purified enzyme determined by gel filtration was 95,000 +/- 5,700 and the subunit molecular weight was 48,000 +/- 2,100. The enzyme showed absorption maxima at 282, 330, and 414 nm and contained only 1 mol of pyridoxal 5'-phosphate/mol of dimer. The pH optimum for enzyme activity was 8.8 and the Km values for beta-alanine and 2-oxoglutaric acid were calculated to be 3.9 and 1.4 mM, respectively. The enzyme catalyzed transamination of various omega-amino acids with 2-oxoglutaric acid, which was a favourable amino acceptor. beta-Alanine, gamma-aminobutyric acid, and beta-aminoisobutyric acid, which are naturally occurring substrates, were preferred amino donors, but taurine, alanine, ornithine, spermine, and spermidine were not. 6-Azauracil inhibited the enzyme activity with a Ki of approximately 1.5 mM. From the above properties, beta-alanine aminotransferase from rabbit liver was seen to closely resemble with 4-aminobutyrate aminotransferase from liver and brain.
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PMID:Purification and properties of beta-alanine aminotransferase from rabbit liver. 681 89

To investigate the considerable variation in stimulation of serum aminotransferase activities by pyridoxal-5'-phosphate added in vitro, we determined the pyridoxal-5'-phosphate content of plasma, using the tyrosine decarboxylase reaction together with the catalytic activities of alanine aminotransferase and aspartate aminotransferase, with and without pyridoxal-5'-phosphate supplementation, within a group of normal human individuals. We found a very significant inverse linear relationship between plasma pyridoxal-5'-phosphate concentration and stimulation of the activities of these enzymes in serum after supplementation with pyridoxal-5'-phosphate. We conclude that the degree of stimulation of the apoenzyme of the two serum aminotransferases clearly depends on the pyridoxal-5'-phosphate concentration in vivo.
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PMID:Apoenzyme content of serum aminotransferases in relation to plasma pyridoxal-5'-phosphate concentration. 683 55

Aspartate aminotransferase (AST) determinations in erythrocytes of patients undergoing chronic haemodialysis and with kidney transplants showed that patients receiving vitamin B6 had a smaller relative stimulation rate of AST by pyridoxal-5'-phosphate (P-5-P). In contrast to these results in erythrocytes, the apoAST and apo-alanine aminotransferase (ALT) activities in serum were increased in patients as compared with those of healthy persons. The corresponding relative stimulation rates of AST and ALT by P-5-P addition to the reaction mixture were not changed in the haemodialysis patients, but in renal transplant recipients the relative stimulation rate of AST was significantly smaller and that of ALT was greater.
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PMID:On the pyridoxal-5'-phosphate stimulation of aspartate aminotransferase and alanine aminotransferase in serum and erythrocytes of patients undergoing chronic haemodialysis and with kidney transplants. 702 88


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