Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.4.1.2 (glutamate dehydrogenase)
 4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The widely used activity expressions for enzyme levels in tissues are discussed: microkatals per unit of tissue weight, protein weight, and DNA weight. The expression of microkatals present in a definite organ in reference to a standard animal weight, 100 g in the case of rat, is also used. The different expressions are applied to aspartate transaminase, glutamate dehydrogenase and AMP deaminase activities in liver, hind leg striated muscle and kidneys in rat. The conclusion is reached that measurements of enzyme activity in tissues should be expressed in more than one form, as the information drawn from one could differ substantially from that obtained from other, giving artifactual views of the metabolic role played by the enzyme in a given tissue.
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PMID:Different expressions for enzyme activities in organs of rat. Application to aspartate transaminase, glutamate dehydrogenase and AMP-deaminase. 72 35

Urea cycle enzymes are all shown to be active in dolphin liver. Acetylglutamate-independent cytoplasmic carbamylphosphate synthase is also present. Arginase is a basic protein, although less markedly basic than the dog enzyme. It is 118 per cent activated by heating at 50 degrees. Optimum pH is 10.5. Co++ and Ni++ inhibit the enzyme. AMP deaminase, glutamicoxaloacetic transaminase, glutamate dehydrogenase and ornithine transaminase are also active in dolphin liver.
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PMID:Urea cycle enzymes in the liver of a dolphin Platanista indi. 95 55

The present study deals with the effect of atrazine on nitrogen metabolism in the liver and brain of fish. Significant changes were seen in the levels of proteins, free amino acids, ammonia, urea, glutamine and the activity levels of proteases, glucogenic aminotransferases, branched-chain aminotransferases, glutamate dehydrogenase, glutaminase, arginase, AMP deaminase and adenosine deaminase in both the tissues of fish exposed to sublethal concentration of atrazine. The study reflects a shift in nitrogen concentration of atrazine. The study reflects a shift in nitrogen metabolism in the tissues of fish for efficient mobilization of end products of protein catabolism as a consequence of atrazine.
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PMID:Modulations in nitrogen metabolism in the hepatic and neuronal tissues of fish, Tilapia mossambica exposed to atrazine. 185 31

Effects of stretching on muscle amino acids were tested in unloaded soleus by casting the foot in dorsiflexion on one limb of tail-casted, hindquarter-suspended rats. For comparison with unloading, amino acids also were measured in shortened extensor digitorum longus (EDL) in the same casted limb and in denervated leg muscles. Concentrations of tyrosine and glutamate were lower, while aspartate, ammonia, and the ratio of glutamine to glutamate were greater in the stretched than in the freely moving, unloaded soleus, but stretched did not differ from weight-bearing, control muscle. Therefore, stretching the soleus muscle prevented changes in certain amino acids due to unloading. Aspartate, ammonia, glutamine, and the ratio of glutamine to glutamate were lower in the shortened EDL than in the freely moving muscle of the contralateral limb, or in the control muscle. When denervated, these leg muscles also showed lower aspartate, ammonia, and ratio of glutamine to glutamate relative to innervated muscles. Since muscle shortening or denervation produced amino acid changes that mimicked the effects of unloading on the soleus, these responses must reflect the effect of muscle disuse. These data suggested that lower ammonia might cause the lower ratio of glutamine to glutamate with disuse. Because the fresh muscle energy charge, one factor which controls AMP deaminase, generally was not affected by disuse, altered deamination of glutamate via glutamate dehydrogenase may explain the variations in muscle ammonia.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effects of stretching and disuse on amino acids in muscles of rat hind limbs. 256 86

Effects of repeated administration of benthiocarb on the nitrogen metabolism of hepatic and neuronal systems have been studied. Repeated benthiocarb treatment was associated with significant decrease in proteins with a concomitant increase in free amino acids (FAA) and specific activity levels of proteases suggesting impaired protein synthesis or elevated proteolysis. The glycogenic aminotransferases showed a significant elevation in both the tissues indicating high feeding of ketoacids into oxidative pathway for efficient operation of TCA cycle to combat energy crisis during induced benthiocarb stress. However, the activity levels of branched-chain aminotransferases decreased suggesting their reduced contribution of intermediates to TCA cycle. A comparative evaluation of the activity levels of ammonogenic enzymes, AMP deaminase, adenosine deaminase and glutamate dehydrogenase (GDH) indicated that ammonia was mostly contributed by nucleotide deamination rather than by oxidative deamination. GDH exhibited reduced activity due to low availability of glutamate. In accordance with increased levels of urea, the activity levels of arginase, a terminal enzyme of urea cycle was increased suggesting increased urea cycle operation in order to combat the increased ammonia content. As the presence of urea cycle in the brain is rather doubtful, the conversion of ammonia to glutamine for the synthesis of GABA is envisaged in brain whereas in liver, excess ammonia was converted to urea through ornithine-arginine reacting system. The increased glutaminase activity observed during benthiocarb intoxication is accounted for counteracting acidosis or maintenance of metabolic homeostasis. Arginase, a terminal enzyme of ornithine cycle showed increased activity denoting the efficient potentiality of tissues to avert ammonia toxicity. The changes observed in tissues of rat administered with benthiocarb reflects a shift in nitrogen metabolism for efficient mobilization of end products of protein catabolism.
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PMID:Perturbations in nitrogen metabolism of brain and liver of rat following repeated benthiocarb administration. 266 46

Anaesthetized rats were given an i.v. overload of 200 mmoles of ammonium acetate. Plasma ammonium levels were not altered for up to 20 minutes after the end of the infusion. The load of ammonium, however, increased the overall non-protein nitrogen content of circulating plasma, as for the increase in urea and amino acids (alanine, phenylalanine, aspartate + asparagine and glutamate + glutamine). The activities of glutamine synthetase was found increased in liver, muscle and kidney; and glutamate dehydrogenase increased in liver and decreased in muscle and kidney. Adenylate deaminase decreased in all the studied tissues. The fast enzyme and plasma metabolite adaptations to ammonium overload were all in the sense of favoring the incorporation of ammonium into amino acids (later into urea) as well as to avoid their deamination, thus effectively removing the excess ammonium from the bloodstream.
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PMID:Rapid detoxification of infused ammonium by the anesthetized rat. 290 36

Denervated dog gastrocnemius muscle has shown a progressive decrease in total protein content, alanine aminotransferase (AIAT), aspartate aminotransferase (AAT) and glutamate dehydrogenase (GDH) activity levels and elevation in free amino acid, ammonia, urea, glutamine contents and AMP deaminase activity levels during post-neurectemic days. The possible implications of these findings are discussed in relation to denervation atrophy.
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PMID:Skeletal muscle protein metabolism under denervation atrophy in dog, Canis domesticus. 357 Apr 36

A method for measuring free fatty acids by enzymic cycling is described. Free fatty acids are converted to acyl-CoAs by acyl-CoA synthetase, then the acyl-CoAs are hydrolyzed back to the free fatty acids by acyl-CoA hydrolase in a cyclic fashion. The amounts of AMP produced during this cyclic reaction are determined from the absorbance at 340 nm in the presence of AMP deaminase and glutamate dehydrogenase. This method is sensitive to as low as 0.1 nmol of free fatty acids, and the standard curve is linear up to 1.0 nmol. This method shows a broad specificity for long-chain fatty acids (C12--C20) and the recoveries of fatty acids added to bacterial cell-free extracts are more than 90%.
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PMID:An enzymic cycling method for the determination of free fatty acids with acyl-CoA synthetase and acyl-CoA hydrolase. 613 47

Lactate (LDH) and succinate (SDH) dehydrogenases activities decreased in red and white muscles of rat under acute ethanol loading indicating the inhibition of energy metabolism and stepped up lactic acid formation under stress conditions. Aspartate aminotransferase (AAT) and glutamate dehydrogenase (GDH) were found to increase. In contrast to these, the AMP deaminase activity decreased in white muscle suggestive of decreased deamination of nucleic acids. The ornithine cycle enzymes such as argininosuccinate synthetase (ArSS) and arginase indicated diminished activities showing low level of operation of urea cycle and consequent accumulation of ammonia was observed in red muscle with low production of glutamine, whereas in the case of white muscle this trend is reversed. The possible alterations of ethanol toxicity on energy requirements, transdeamination patterns, ureogenesis and glutamine production have been discussed.
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PMID:Metabolic alterations in the red and white muscles of rat to acute ethanol treatment. 618 32

Lactate dehydrogenase (LDH), succinate dehydrogenase (SDH), aspartate aminotransferase (AAT), glutamate dehydrogenase (GDH), AMP deaminase, ornithine transcarbamylase (OTC), arginase and glutamine synthetase (GS) activities were increased in the kidney of the rat during repeated ethanol loading. The significance of these findings is discussed.
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PMID:Renal ammonia metabolic response in the rat to repeated ethanol loading. 648 7


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