Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Gene frequencies of common and rare GPT alleles derived from an investigation of 1139 unrelated, healthy individuals from southwestern Germany are given. GPT typing was performed by means of horizontal starch gel electrophoresis in a Tris-histidine x HCl buffer system. In addition, a new electrophoretic variant, GPT9, is described. The frequencies of the GPT alleles observed were calculated as: GPT1, 0.4987; GPT2, 0.4686; GPT1M, 0.022; GPT0, 0.005; GPT3, 0.0022; GPT4, 0.0025; GPT8, 0.0005; GPT9, 0.0005.
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PMID:Polymorphism of alanine aminotransferase (E.C.2.7.6.1): common and rare alleles. 51 Nov 57

Effects of pregnancy superimposed upon a rapid phase of growth in the rat on the vitamin B-6 needs during gestation were examined. Rats were fed 1.2, 2.4, 4.8, 9.6, or 19.2 mg pyridoxine-HCl/kg diet from weaning. Some animals from each dietary treatment were mated at 55 (P-55) and 115 (P-115) days of age; others of the same ages served as nonpregnant controls. Analyses were made on day 21 of gestation. Excepting the 1.2-mg diet treatment, maternal weight gains during gestation were greater for P-55 groups compared with gains of the P-115 groups, possibly reflecting maternal growth. Both maternal weight gains and fetal weights were less for the 1.2-mg, P-55 group; otherwise reproductive performance was similar among the groups. On the basis of stimulation of erythrocyte alanine aminotransferase activity by pyridoxal phosphate added in vitro, the needs in all pregnant and nonpregnant groups were met by 2.4 mg pyridoxine/kg diet. However, on the basis of vitamin B-6 saturation of tissues, the pyridoxine needs were 9.6 mg/kg diet for young growing animals and 4.8 mg/kg diet for older animals in which growth had almost ceased. The needs for both young and older pregnant animals possibly exceeded 19.2 mg pyridoxine/kg diet for vitamin B-6 saturation of maternal liver, fetus, and fetal brain. Pregnancy superimposed upon a rapid phase of growth in conjunction with a restricted intake of pyridoxine resulted in low values for most parameters used in the assessments compared with values for animals fed the same vitamin level but mated after growth velocity had diminished.
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PMID:Effects of different levels of pyridoxine fed during pregnancy superimposed upon growth in the rat. 112 71

Response characteristics are presented for a dual-enzyme fiber-optic biosensor for glutamate. An enzyme layer composed of glutamate dehydrogenase (GDH) and glutamate-pyruvate transaminase (GPT) is used to produce reduced nicotinamide adenine dinucleotide (NADH) at the tip of a fiber-optic probe. NADH luminescence is monitored through this probe and the measured fluorescence intensity is related to the concentration of glutamate. GDH catalyzes the formation of NADH, and GPT drives the GDH reaction by removing a reaction product and regenerating glutamate. Optimal response is obtained in a pH 7.4 Tris-HCl buffer maintained at 25 degrees C in the presence of 4 mM NAD+ and 10 mM L-alanine. The temperature profile reveals a strong negative temperature effect which is attributed to the temperature dependency of NADH luminescence. Under optimal conditions, the sensor sensitivity is 0.127 nA/microM over the 1-10 microM concentration range, the detection limit is 0.13 microM, and response times range from 4 to 8 min. The sensor response is stable for 12 days when stored at 4 degrees C. Selectivity for glutamate is excellent over most of the common amino acids as well as ascorbic acid, uric acid, taurine, and GABA. Only slight responses were observed for glutamine and lysine. The effect of ammonia on the glutamate response was found to be minimal at total ammonia nitrogen concentrations as high as 200 microM.
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PMID:Dual-enzyme fiber-optic biosensor for glutamate based on reduced nicotinamide adenine dinucleotide luminescence. 135 Apr 33

The study embraces the shops: metallurgic, electrolysis, production of sulfuric acid and shop 100. Tests are performed on the environmental pollution by dust, sulfur dioxide, chlorine, aerosols of sulfuric acid, carbon monoxide, nitric oxide and dioxide, hydrogen chloride, arsenic (II) oxide (III), selenium, tellurium and metal aerosols: lead, copper, cadmium and zinc. The total concentrations of chemical noxae, generating multicomponent mixtures with one-way effect on the work place, are reckon, and estimation in the Bulgarian Institute of Hygiene and Occupational Health and the Ministry of public health methods. In the same shop is comprised a representative group of workers with paraclinical tests: GOT and GPT activity, content of copper and zinc in blood. The assessment made on the work conditions and the changes already found in the workers lead to a discussion for optimizing the conditions in the new shops for copper production.
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PMID:[Hygienic evaluation and the effects of toxic factors in the work environment of copper-processing plants]. 263 3

We compared the vitamin B-6 status of 12-wk-old rats (n = 12) fed excess (1400 mg/kg diet) or the recommended level (7 mg/kg diet, control) of pyridoxine (PN) hydrochloride to test if excess vitamin B-6 would cause tissue depletion of pyridoxal phosphate (PLP), the active coenzyme form of vitamin B-6. Plasma PLP, tryptophan-load test results, food intake, and tissue and body weights were not different at wk 6. Red blood cell endogenous alanine aminotransferase activity and PLP concentration were elevated (P less than 0.01) in rats fed 1400 mg PN.HCl/kg diet. In contrast, PLP concentration in muscle was significantly lower (P = 0.01) in rats fed excess vitamin B-6 (9.7 +/- 0.8 nmol/g, mean +/- SEM) than in controls (14.9 +/- 1.4). PLP concentration in other tissues, including plasma, was not affected. In rats fed excess vitamin B-6, pyridoxal was increased in all tissues examined (P less than 0.05), and total vitamin B-6 was increased in plasma, red blood cells and kidneys (P less than 0.05). Total glycogen phosphorylase (a + b) activity in the gastrocnemius was not affected, but phosphorylase a activity was increased in rats fed excess vitamin B-6 (P = 0.025). Concentrations of dopamine and metabolites in the caudate nucleus of the basal ganglia were not affected. A transient, but significant, elevation in acoustic startle response, a central nervous system reflex, was observed in rats fed excess vitamin B-6. The depletion in muscle PLP could not hae been predicted by either plasma or red blood cell PLP concentration, although the latter did reflect vitamin B-6 intake.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Evaluation of vitamin B-6 status and function of rats fed excess pyridoxine. 268 1

Short-term treatment of rats with hepatocarcinogens elicits a consistent pattern of phenotypic changes in hepatic drug metabolizing enzymes, the most striking of which is a marked increase in microsomal epoxide hydrolase (EH) activity. The antihistaminic drug methapyrilene induces a high incidence of hepatocellular carcinoma in F-344 rats. The studies reported here were designed to assess the effects of methapyrilene on hepatic EH activity, cytochrome P-450-dependent mixed-function oxidase activities, liver morphology, and liver-derived serum enzymes. Male F-344 rats were treated with three daily oral doses of methapyrilene-HCl, up to 300 mg/kg/day, and were sacrificed 48 hr after the last dose. Hepatic microsomal EH and cytosolic DT-diaphorase activities were increased in a dose-related fashion, to 420 and 230% of control, respectively. Cytochrome P-450 content and benzphetamine-N-demethylase and ethoxycoumarin-O-deethylase activities were concomitantly decreased to 35-50% of control. Serum gamma-glutamyl transpeptidase and alanine aminotransferase activities were elevated 22- to 27-fold, and serum bile acids to 36-fold by treatment with methapyrilene. Periportal lesions, characterized by inflammation, nuclear and nucleolar enlargement, bile duct hyperplasia, and hepatocellular necrosis, were observed following methapyrilene administration. The severity of the periportal lesion correlated with elevations in the serum chemistry parameters. The increases noted in microsomal EH activity supports the suggestion that this enzyme may be a useful biochemical marker for exposure to hepatocarcinogens.
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PMID:Effects of methapyrilene on rat hepatic xenobiotic metabolizing enzymes and liver morphology. 285 28

During an evaluation of the IFCC reference method for alanine aminotransferase (ALT, EC 2.6.1.2), we noted that the specimen blank activity reaction was markedly increased. Experience with five different lots of D-alanine from four commercial sources indicated that substantial and varying negative bias (up to -10%) could be introduced into the blank-corrected ALT activity, depending on the lot of D-alanine used. Although the IFCC procedure for ALT mentions the possibility of this L-alanine contamination, we believe that the degree of contamination in commercial reagents is underestimated. Analyzing the five lots of D-alanine for L-alanine, we found the magnitude of negative bias to be correlated directly with L-alanine contamination. Here, we describe a quick, sensitive assay based on coupled reactions of L-amino acid oxidase/peroxidase for quantifying L-alanine in the concentration range of 0-15 mmol/L without a sample-dilution step. Results by this alternative L-alanine assay agreed well with those recommended in the IFCC ALT procedure. Further examination suggested an even simpler solution to the L-alanine contamination problem, because we found no difference in the blank-corrected ALT activity determined in Tris HCl buffer, with or without D-alanine (free of L-alanine). We therefore propose that D-alanine be omitted from the IFCC reference ALT procedure.
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PMID:Evaluation of the IFCC reference method for alanine aminotransferase: spurious blank ALT activity due to contamination of D-alanine with L-alanine, and recommendations for a correction. 291 May 58

Effects of lidocaine on organ localization of neutrophils and bacteria and on hemodynamic and metabolic variables were determined during septic shock in dogs. Twelve anesthetized dogs were infused with 10(10) Escherichia coli/kg of body weight through a portal vein catheter over a 1-hour period. Six of these 12 dogs were treated with 2 mg of lidocaine HCl/kg (6 mg/kg/h) 15 minutes after the bacterial infusion had begun. Six dogs not given E coli (surgical controls) were given saline solution at the same rate as the bacterial and lidocaine infusions. Over 4 hours, nontreated dogs with septicemia developed systemic hypotension, decreased cardiac output, increased portal pressure, increased serum alanine transaminase activity, increased liver extravascular water, increased liver glycogen depletion, and decreased PaO2, compared with control dogs. Accumulations of polymorphonuclear leukocytes and E coli were found in the liver and lungs of dogs with septicemia. Lidocaine treatment did not alter the hemodynamic measurements and resulted in metabolic acidosis and hypoalbuminemia. Decreased numbers of E coli were recovered from the liver of lidocaine-treated dogs, whereas increased numbers of organisms were recovered from the blood. Neutrophil sequestration was increased in the liver, but not the lungs of lidocaine-treated dogs.
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PMID:Lidocaine treatment of dogs with Escherichia coli septicemia. 328 25

We examined 17 lots of 2-oxoglutarate (seven acid forms, three K salt forms, and seven Na salt forms), obtained from eight commercial suppliers, for suitability for measuring aspartate aminotransferase (EC 2.6.1.1) and alanine aminotransferase (EC 2.6.1.2) in human serum. Measurements of the catalytic activity concentrations of these two aminotransferases with each of these 17 preparations were not sufficiently sensitive to distinguish good from poor-quality material. Thus, we ranked these lots for purity, by specific analysis with glutamate dehydrogenase and by liquid chromatography, and determined the water content, acid content, and spectral characteristics of each. On the basis of a 2-oxoglutarate assay value by glutamate dehydrogenase of 98% or greater, we considered seven of the preparations acceptable and 10 unacceptable. The molar absorptivities (L X mol-1 X cm-1, mean +/- SD) of the seven acceptable lots in 1 mol/L HCl were: epsilon 325 nm = 9.12 +/- 0.02 (CV = 0.2%), epsilon 279 nm = 2.63 +/- 0.23 (CV = 9.9%), and epsilon 245 nm = 37.9 +/- 4.1 (CV = 10.9%). Use of these spectrophotometric limits alone unambiguously distinguished the inferior lots of 2-oxoglutarate. We urge the inclusion of detailed spectrophotometric specifications for 2-oxoglutarate in Reference Methods for aminotransferase measurements.
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PMID:Comparisons of 17 lots of 2-oxoglutarate, and specifications for use of this substrate in reference methods. 399 57

The activity of alanine aminotransferase (ALT) phenotypes was determined in 148 hemolysates of the Serbian population. The highest activity was obtained for phenotype ALT 1 (0.614 U/g Hb), intermediate for ALT 2-1 (0.475 U/g Hb), and the lowest for ALT 2 (0.395 U/g Hb). To explain the differences in catalytic activity between the ALT phenotypes, some kinetic characteristics were investigated. No difference in heat stability and calculated activation energies for ALT phenotypes could be detected. Addition of pyridoxal 5'-phosphate to the reaction system did not increase the catalytic activity. For the catalytic activity of all three phenotypes, a broad pH optimum in the range 7.1 to 7.6 was found. The Tris/HCl buffer concentration of 140 mmol/liter was optimal. The Michaelis-Menten constants for L-alanine as substrate were 2.462 mmol/liter for ALT 1, 1.965 mmol/liter for ALT 2-1, and 2.698 mmol/liter for ALT 2. For another substrate, 2-oxoglutarate, Km values were 0.299, 0.208, and 0.202 mmol/liter, respectively.
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PMID:Some kinetic characteristics of erythrocyte alanine aminotransferase phenotypes. 400 95


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