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

The stabilities of nine rat liver cytosol enzymes were compared at a variety of pH values. The cytosol enzymes studied were (a) those with half-lives in vivo of 3 days or longer: lactate dehydrogenase, arginase, glyceraldehyde phosphate dehydrogenase and alanine aminotransferase, (b) those with half-lives in vivo shorter than 2 days; glucokinase, dihydroorotase, serine dehydratase and tyrosine aminotransferase and (c) catalase, which has an intermediate half-life of 2.5 days for the protein protion. All the enzymes were stable in vitro at neurtal and alkaline pH values. However, at acidic pH values (pH 4): the long-lived enzymes (a) were stable; the short-lived enzymes (b) were completely inactivated with one exception; and catalase was partially inactivated. Tyrosine aminotransferase was the exception in that it is a short-lived enzyme in vivo but stable under all conditions tested in vitro. The finding that long-lived enzymes are stable in an acid milieu and short-lived enzymes are generally unstable was only observed if certain ligands (NAD+, pyridoxal 5'-phosphate, Mn2+, amino acids) were added to the invitro system. Lysosomal extracts did not accelerate the rate of inactivation of any cytosol enzyme in acidic solutions. These results indicate that if degradation of intracellular enzymes occurs in lysosomes, acid inactivation and denaturation of enzymes may be the initial event in determining the functional half-lives of the enzymes in vivo.
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PMID:Acid inactivation of short-lived rat liver enzymes. 1 3

We report the intermediate-term effects of three consecutive evenings of moderate ethanol ingestion (0.75 g/kg body weight each evening) on activity values for alkaline phosphatase, gamma-glutamyltransferase, creatine kinase, aspartate aminotransferase, alanine aminotransferase, and lactate dehydrogenase in sera of nine apparently healthy young adults. We define "intermediate-term" effects as those occurring between 10 h and 100 h after completion of the ethanol consumption schedule. The most pronounced changes in enzyme activity for the group of volunteers were: gamma-glutamyltransferase, +25% at 60 h after ethanol ingestion; alanine aminotransferase, +12% at 60 h after ethanol; and aspartate aminotransferase,--12% at 60 h after ethanol. All three enzymes exhibited similar time courses, i.e., mean peak activity changes were observed at 60 h, and all three mean enzyme activity values returned to near baseline by 100 h. The possible explanations for the observed changes and the clinical significance are discussed.
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PMID:The effects of ethanol (0.75 g/kg body weight) on the activities of selected enzymes in sera of healthy young adults: 1. Intermediate-term effects. 1 40

Intensive care patients receiving prolonged total parenteral nutrition (TPN) developed alterations of liver function tests, seen in the activity of certain serum enzymes. Hepatomegaly and jaundice sometimes appeared. The changes in chemical pathology were in serum transaminases activity (GOT, GPT, GDH); alkaline phosphatase and gamma-glutamyltranspeptidase as indices of cholestasis; lactate dehydrogenase, hydroxybutyrate dehydrogenase and creatine phosphokinase, as enzymes related to energy metabolism; pseudocholinesterase, as a protein metabolism-related enzyme. The possible causes of these alterations in critically ill patients undergoing TPN are considered and a functional final metabolic interpretation is proposed.
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PMID:Metabolic changes during prolonged total parenteral nutrition in intensive care. 3 24

We have determined the distribution in cord blood from healthy newborns of six enzymes: creatine kinase, lactate dehydrogenase, aspartate and alanine aminotransferase, alkaline phosphatase and gamma-glutamyltransferase. The concentration of enzymes were determined according to the methods recommended by the Scandinavian Committee on Enzymes. The distribution of isoenzymes and of enzymes in blood from women at delivery was investigated also. All distributions were positively skewed. The upper reference limits of cord blood exceeded those found in mother blood by a factor of eight for gamma-glutamyltransferase, and for lactate dehydrogenase and creatine kinase by a factor of two.
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PMID:Reference values for six enzymes in plasma from newborns and women at delivery. 4 84

The relationship between plasma protein bound iodine (PBI) level and creatine kinase (CK) activity was investigated in 143 males and 528 females suspected of various thyroid disorders; there was significant negative correlation between low PBI level and raised CK activity. CK, aldolase, lactate dehydrogenase (LD), aspartate transaminase (AST), and alanine transaminase (ALT) activities were determined in plasma from patients with reduced PBI levels; apart from CK, LD was the only enzyme increased in an appreciable number of cases. A further series of specimens was collected from 66 patients with low PBI levels and the CK isoenzymes investigated. In all of these MM was the main form present; a trace of MB was found in 6. These findings do not explain the elevation of CK in hypothyroidism which may be a non-specific effect.
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PMID:An investigation into creatine kinase and other plasma enzymes in thyroid disorders. 7 98

Normal values for a number of blood components of grivet monkeys are reported. Haematological data and values for glucose, cholesterol and urea are similar to those of rhesus monkeys. Activities of alkaline phosphatase (1526 U/l), glutamine oxaloacetate transaminase (30.9 U/l), glutamine pyruvate transaminase (13.7 U/l), lactate dehydrogenase (629 U/l), alpha-hydroxybutyrate dehydrogenase (175 U/l), creatine phosphokinase (227 U/l), gamma-glutamyl transpeptidase (38.7 U/l) and sorbitol dehydrogenase (14.2 U/l), and levels of lysozyme (178 mg/dl), zinc (162 microgram/dl), copper (81.3 microgram/dl) and iron (296.5 microgram/dl) have not previously been reported for this animal. Values for serum amino acids, proteins, electrolytes, triglycerides and creatinine are compared with those of other primates.
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PMID:Normal values for some whole blood and serum components of grivet monkeys (Cercopithecus aethiops). 11 24

Adaptation of Ehrlich ascites tumor cells to serial cultivation in media with progressively elevated (hypertonic) NaCl content ("high NaCl"-tolerant cells) has resulted in progressive increases of the cellular activities of NAD-dependent glycerol-3-phosphate dehydrogenase (EC 1.1.1.8), NAD-dependent malate dehydrogenase (EC 1.1.1.37), glutamate--oxalacetate transaminase (EC 2.6.1.1), NAD (P)-dependent glutamate dehydrogenase (EC 1.4.1.3), NADP-dependent isocitrate dehydrogenase (EC 1.1.1.42). The activities of glutamate-pyruvate transaminase (EC 2.6.1.2.) and of glycolytic enzymes as phospho-fructokinase (EC 2.7.1.11), glyceraldehydephosphate dehydrogenase (EC 1.2.1.12) and lactate dehydrogenase (EC 1.1.1.27) were only slightly and not in progressive manner (in response to the progressive increase of the environmental NaCl concentration) affected. These changes are discussed with respect to a metabolic pattern of these "high NaCl"-tolerant cells which is compatible with increased energy requirements, especially for active cation transport. It is suggested that these increased cellular enzyme activities reflect an increased transfer of reducing equivalents across mitochondrial membranes (via the "glycerophosphate cycle and the malate-aspartate shuttle") and possibly a stimulated lipid metabolism. These alterations in the level of enzyme activities must be regarded asan adaptive cellular response to the "high NaCl" environment, since readaptation to growth in regular isotonic media resulted in a reversion to the enzyme pattern characteristic of the parent cells.
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PMID:Changes in enzyme pattern of Ehrlich ascites tumor cells following serial cultivation in media with increased (hypertonic) NaCl content. 12 1

We investigated the enzyme activity of the blank in the spectrophotometric determination of the aminotransferase activities and aspartate aminotransferase activity. 6 lactate dehydrogenase and 3 malate dehydrogenase preparations from different manufactures and from different organs showed additional and contaminating activity. The additional activity depends upon the 2-oxoglutarate concentration. The contaminating activity is caused by alanine aminotransferase and aspartate aminotransferase in the auxiliary enzymes. We propose that exact definitions must be given for the auxiliary enzymes in the recommendations of standard determinations for enzyme activities.
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PMID:Influence of auxiliary enzymes on the spectrophotometric measurement of alanine aminotransferase and aspartate aminotransferase activities. 17 28

In the experiments performed with broilers, after a per os application of tetrachloromethane and cadmium (Cd+2), the activity of lactate dehydrogenase (LDH), leucylarylamidase (LA), and the GOT and GPT amino transferase was determined in the blood plasm. By means of an electrophoretic division of the blood plasm of clinically healthy broilers one enzymatically active fraction of LA and LDH was ascertained. The injury caused to the organism of poultry by carbon tetrachloride and cadmium did not affect the heterogeneity of these two enzymes. After an application of tetrachloromethane (CCl4) in the dose of 8 and 10 ml kg-1 the total activity of LDH and LA changed. The influence of cadmium on the organism in the total dose of 200 mg kg-1 resulted in the changed activity of LDH, GOT, and LA. From the results obtained it has been assumed that the examined activity of LDH, GOT, and LA can be utilized for the diagnosing of non-specific injuries of the organism of poultry.
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PMID:[Dynamics of changes in the activity of plasma lactate dehydrogenase, leucylarylamidase and GOT and GPT aminotransferases in poultry following damage to the organism caused by cadmium and tetrachloromethane]. 18 Jun 43

Enzyme activity of lactate dehydrogenase, glutamate-oxalacetate and glutamate-pyruvate transaminase, creatine phosphokinase, cholinesterase, alkaline, acid and prostatic phosphatase and aldolase has been studied in a total of 213 subjects, of whom 97 were of good health, 63 had bone tumors and 53 suffered from osteomyelitis. The activities of the majority of the enzymes were found to become significantly changed in comparison with the norm. In both patient groups, the more striking differences being noted in that of osteomyelitis. However, enzymatic activity alone does not allow to differentiate the group of bone tumors from that of osteomyelitis, the differences between these two groups not being of significance in any one of the enzymes followed.
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PMID:Serum enzyme activity in bone tumors and osteomyelitis (LDH, GOT, GPT, CPK, CHE, ALP, AP, PP, ALD). 19 May 48


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