Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.5.4.17 (adenosine deaminase)
 5,206 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

High-performance liquid chromatography (HPLC) coupled to an electrochemical detector in an oxidative mode was used to analyze purine bases, nucleosides, and nucleotides as well as restriction fragments of nucleic acids. Ligands were separated by liquid chromatography with electrochemical detection (LC-EC) using size exclusion, ion-exchange, or reverse phase techniques. Using an amperometric electrochemical detector the determination was characterized with respect to sensitivity, selectivity, and capacity factor. It was observed from hydrodynamic and cyclic voltammetry that the optimum oxidation potential differed for the three major classes of purines, permitting an enhancement in selectivity when compared to detection. Guanylyl moieties demonstrated a half-wave potential at 0.800 V vs Ag/AgCl, while those for the adenylyl and inosylyl groups are above 1,000 V vs Ag/AgCl. The facility of the method to analyze components of a complex biological milieu was demonstrated by examining the purine pools of crude and partially purified eye lens homogenates as well as by comparing the traditional hexokinase assay to the newly developed LC-EC technique. Additionally, LC-EC was compared to detection for determination of the purine-metabolizing enzyme activities, adenylate deaminase and adenylosuccinate synthetase from crude cellular lysates of the cellular slime mold, Dictyostelium discoideum. Finally, the technique was used to assay the fragments from lambda-DNA cut with the restriction endonuclease Pst-1.
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PMID:LC-EC determination of nucleotides and nucleic acids: application to enzyme assays and the analysis of DNA fragments. 283 15

Adenosine is a local hormone and is considered to act as a vasodilatory substance when released locally. Alcohol is known to affect membrane structure and acts as a coronary vasodilator. Membrane enzymes such as 5'-nucleotidase, adenosine deaminase, and gammaglutamyl transpeptidase, along with AMP deaminase, have been studied in rat myocardial tissue following the administration of a sufficiently toxic dose (producing semiconsciousness) of ethanol (1ml of 7M ethanol/100g body wt.). The activity of 5'-nucleotidase as well as that of adenosine deaminase increased due to the administration of ethanol, without any significant change in the activities of gammaglutamyl transpeptidase and AMP deaminase. These changes are discussed in relation to the metabolic changes occurring in the myocardium and the resultant effects on the coronary vessels.
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PMID:Acute effects of ethanol on production & disposal of adenosine from rat myocardium. 285 55

Activities of alanine and aspartate transaminases, glutamine synthetase, adenylate deaminase, glutamate and xanthine dehydrogenases and lactate dehydrogenase were measured in leg and breast muscles of developing chicks from day 10 in ovo to day 5 of free life, and compared with measurements for adult hens. Xanthine dehydrogenase activity was low in both muscles with adult levels attained on day 15 in ovo. Glutamine synthetase for chicks was maintained higher during development than for adults in both muscles. Minor differences were observed between both muscles in all enzymes tested up to day 18. With low embryonic values and important rises before hatching, the differences were initiated in the posthatching period. Important differences were observed between adult levels of activity. Leg muscle revealed higher enzyme values except for lactate dehydrogenase and indistinguishable levels for adenylate deaminase and xanthine dehydrogenase in both muscles. Alanine, instead of glutamine, is postulated as the main nitrogen transport between muscle and liver in the domestic fowl.
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PMID:Patterns of amino acid enzyme in domestic fowl breast and leg muscle during development. 286 43

The activities of aspartate and alanine transaminase, serine dehydratase, arginase, glutamate dehydrogenase, adenylate deaminase and glutamine synthetase were determined in the stomach and small intestine of developing rats. Despite the common embryonic origin of the intestine and stomach, their enzymes showed quite different activity levels and patterns of development, depending on their roles. Most enzyme activities were low during late intrauterine life and after birth, attaining adult levels with the change of diet at weaning. No arginase activity was found in the stomach and no changes were detected in adenylate deaminase in the stomach or intestine throughout the period studied. Alanine transaminase, serine dehydratase and, to some extent, glutamine synthetase levels, significantly higher in late intrauterine life, decreased after birth, suggesting that the foetal stomach has a transient ability to handle amino acids.
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PMID:Activities of amino acid metabolizing enzymes in the stomach and small intestine of developing rats. 286 86

There was a nil arginase and serine dehydratase activities in interscapular brown adipose tissue, but the activity of adenylate deaminase, glutamine synthetase, glutamate dehydrogenase and the aspartate, alanine and branched chain amino acid transaminases was higher than those of white adipose tissue; the differences were diminished when expressed per unit of protein weight. Brown adipose tissue enzyme activities were in a range between those of liver and muscle. The high amino acid handling capabilities, together with its physiological role, suggest that brown adipose tissue can metabolize significant amounts of amino acids, its enzyme pattern being different both from white adipose tissue, as well as of liver and muscle.
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PMID:Activities of enzymes of amino acid metabolism in rat brown adipose tissue. 287 38

The enzymes that catalyse the salvage of purines in Entamoeba histolytica trophozoites have been surveyed. Adenine deaminase (EC 3.5.4.2), adenosine deaminase (EC 3.5.4.4), guanine deaminase (EC 3.5.4.3), adenine phosphoribosyltransferase (PRTase) (EC 2.4.2.7), xanthine PRTase (EC 2.4.2.22) and hypoxanthine PRTase (EC 2.4.2.8) were all detected in cell homogenates but only at low activities, whereas AMP deaminase (EC 3.5.4.6) and guanine PRTase (EC 2.4.2.8) were not found. Phosphorylases (EC 2.4.2.1) active in both anabolic and catabolic directions were present and all nucleosides tested were phosphorylated by kinases (EC 2.7.1.15, EC 2.7.1.20, EC 2.7.1.73). 3'-Nucleotidase (EC 3.1.3.6) and 5'-nucleotidase (EC 3.1.3.5) were found, the former being mainly particulate. Nucleotide interconversion enzymes (adenylosuccinate lyase, EC 4.3.2.2; adenylosuccinate synthetase, EC 6.3.4.4; IMP dehydrogenase, EC 1.2.1.14; GMP synthetase, EC 6.3.5.2 and GMP reductase, EC 1.6.6.8) were not detected. The results suggest that in E. histolytica the main route of nucleotide synthesis is from the individual bases through the actions of phosphorylases and kinases.
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PMID:Purine-metabolising enzymes in Entamoeba histolytica. 287 91

The effect of feeding a high-energy highly palatable cafeteria diet on the liver and muscle ontogenesis of serine dehydratase, alanine transaminase, glutamine synthetase and adenylate deaminase during postnatal development of the rat has been studied. The results are in agreement with the lower amino acid utilization in cafeteria rats, both adults and during postnatal development. The feeding of excess energy coupled with high-quality protein resulted in changes in the ontogenesis of the studied enzymes that coincide with the development of protein synthesis and overall pup growth even before they had direct access to this rich diet, suggesting that cafeteria feeding already affects the amino acid metabolism of the pup through the dam's milk.
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PMID:Postnatal development of amino acid metabolism enzymes in the liver and muscle of 'cafeteria' rats. 287 17

The activities of alanine and aspartate transaminases, adenylate deaminase, glutamine synthetase and glutamate and xanthine dehydrogenases have been measured in liver, yolk sac membrane, intestine and breast and leg muscle of domestic fowl hatchlings receiving for 3 or 5 days either a standard diet or hard boiled eggwhite as well as in 3 or 5 days starved animals. The patterns of activation of amino acid metabolism enzymes were fully comparable in protein-fed and starved groups with respect to fed controls; the differences with respect to the latter became more marked in 5- than in 3-days old chicks. In 5-days old chicks intestine alanine transaminase activity increased in parallel to that of liver in protein-fed animals but not in those starved, in agreement with an enhanced alanine transfer between both organs under this situation. Both, starvation and protein-feeding, induced a general decrease in the amino acid metabolizing ability of muscle. Glutamine (but not alanine) synthetizing capabilities were enhanced.
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PMID:Effect of starvation and a protein diet on the amino acid metabolism enzyme activities of the organs of domestic fowl hatchlings. 287 42

The effect of 24-hr starvation on the amino acid pool composition and its concentration ratios with respect to blood and plasma as well as the activities of alanine, aspartate and branched chain amino acid transaminases, glutamate dehydrogenase, glutamine synthetase and adenylate deaminase have been studied in rat brown adipose tissue. Starvation induced a considerable decrease of pool amino acid concentration. Alanine and taurine were the amino acids in which the decrease was more marked. Small changes were observed in the activities of the enzymes studied, with decreases only in glutamate dehydrogenase and adenylate deaminase. These changes agree with a decrease in amino acid utilization in this tissue induced by starvation.
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PMID:Effect of 24-hour starvation on amino acid pool composition and enzyme activities of rat brown adipose tissue. 288 93

The amino acid pool composition and its concentration ratios with respect to blood and plasma, as well as the activities of alanine, aspartate and branched chain amino acid transaminases, glutamine synthetase, adenylate deaminase and glutamate dehydrogenase have been studied in the interscapular brown adipose tissue of control, 12-h cold-exposed and 15-day cold-acclimated rats. Cold temperature affected the amino acid metabolism and pool composition more intensely after 15 days than after 12-h cold-exposure, even though the patterns of change were very similar in both groups. Cold temperatures induced a decrease in glutamine and an increase in glutamate concentration in the tissue. This probably increased the metabolism of branched chain amino acids and caused a decrease in adenylate deaminase activity. It also seemed to increase alanine utilization. We concluded that amino acid metabolism in brown adipose tissue is enhanced by cold temperature acclimation.
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PMID:Effect of cold-temperature exposure and acclimation on amino acid pool changes and enzyme activities of rat brown adipose tissue. 288 9


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