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

---

Query: EC:3.5.1.1 (asparaginase)
2,695 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Forty-eight tumor-free mice and 32 mice bearing Ehrlich ascites tumor were randomized into 2 treatments, Acinetobacter glutaminase-asparaginase (AGA) (600 IU/kg/day for 7 days) and 0.9% NaCl controls, and into 2 or 3 isocaloric diets, normal protein (NP) (20 g protein/100 g diet), high protein (HP) (58 g protein/100 g diet), and zero protein (ZP) (tumor-free mice only). In tumor-free, NP-fed mice, AGA caused percentage reductions (P less than 0.01) in the nitrogen content of liver (50%), intestine (42%), thymus (89%), spleen (75%), and carcass (20%), but HP prevented this effect on intestine and carcass and caused percentage increases in the nitrogen content of liver (53%), intestine (36%), thymus (122%), and carcass (25%). In Ehrlich ascites tumor mice (NP or HP fed) AGA caused markedly lower (P less than 0.01) tumor burdens and increased nitrogen content of intestine (HP), kidney (NP and HP), and spleen (NP and HP). Ehrlich ascites tumor, AGA-treated, HP-fed mice ate 31% less food (P less than 0.01) (compared to NP) but HP resulted in percentage increases in the nitrogen content of liver (18%; P = 0.05), intestine (25%; P less than 0.05), and thymus (164%; P less than 0.01). In the Ehrlich ascites tumor, AGA group the HP diet caused higher hematocrit and serum total protein (both, P less than 0.05). Adverse nutritional effects of AGA seen in normal mice were markedly diminished in tumor-bearing animals. The observed nitrogen-sparing effects of the high protein: energy ratio may be relevant to humans and to other forms of neoplasia and chemotherapy.
...
PMID:Tissue nitrogen-sparing effect of high protein diet in mice with or without ascites tumor treated with Acinetobacter glutaminase-asparaginase. 402 74

l-Asparaginase from Serratia marcescens was found to hydrolyze l-glutamine at 5% of the rate of l-asparagine hydrolysis. The ratio of the two activities did not change through several stages of purification, anionic and cationic polyacrylamide disk gel electrophoresis, and partial thermal inactivation. The two activities had parallel blood clearance rates in mice. l-glutamine was found to be a competitive inhibitor of l-asparagine hydrolysis. A separate l-glutaminase enzyme free of l-asparaginase activity was separated by diethylaminoethyl-cellulose chromatography.
...
PMID:L-glutamine as a substrate for L-asparaginase from Serratia marcescens. 459 Apr 79

1. Activities of asparagine synthetase, asparaginase, glutamine synthetase and glutaminase have been determined in red muscle, white muscle, brain, kidney, liver and gills of goldfish. 2. Muscle and brain show a capacity for net amide synthesis, while liver and gills are capable of both amide synthesis and degradation. 3. These results are consistent with the hypothesis that amide synthesis and degradation functions as a mechanism controlling tissue ammonia levels and ammonia excretion rates.
...
PMID:Nitrogen metabolism in goldfish, Carassius auratus (L.) activities of amidases and amide synthetases in goldfish tissues. 612 4

We isolated pleiotropic mutants of Klebsiella aerogenes with the transposon Tn5 which were unable to utilize a variety of poor sources of nitrogen. The mutation responsible was shown to be in the asnB gene, one of two genes coding for an asparagine synthetase. Mutations in both asnA and asnB were necessary to produce an asparagine requirement. Assays which could distinguish the two asparagine synthetase activities were developed in strains missing a high-affinity asparaginase. The asnA and asnB genes coded for ammonia-dependent and glutamine-dependent asparagine synthetases, respectively. Asparagine repressed both enzymes. When growth was nitrogen limited, the level of the ammonia-dependent enzyme was low and that of the glutamine-dependent enzyme was high. The reverse was true in a nitrogen-rich (ammonia-containing) medium. Furthermore, mutations in the glnG protein, a regulatory component of the nitrogen assimilatory system, increased the level of the ammonia-dependent enzyme. The glutamine-dependent asparagine synthetase was purified to 95%. It was a tetramer with four equal 57,000-dalton subunits and catalyzed the stoichiometric generation of asparagine, AMP, and inorganic pyrophosphate from aspartate, ATP, and glutamine. High levels of ammonium chloride (50 mM) could replace glutamine. The purified enzyme exhibited a substrate-independent glutaminase activity which was probably an artifact of purification. The tetramer could be dissociated; the monomer possessed the high ammonia-dependent activity and the glutaminase activity, but not the glutamine-dependent activity. In contrast, the purified ammonia-dependent asparagine synthetase, about 40% pure, had a molecular weight of 80,000 and is probably a dimer of identical subunits. Asparagine inhibited both enzymes. Kinetic constants and the effect of pH, substrate, and product analogs were determined. The regulation and biochemistry of the asparagine synthetases prove the hypothesis strongly suggested by the genetic and physiological evidence that a glutamine-dependent enzyme is essential for asparagine synthesis when the nitrogen source is growth rate limiting.
...
PMID:Asparagine synthetases of Klebsiella aerogenes: properties and regulation of synthesis. 612 99

The successful long-term use of asparaginase-glutaminase reactor in dogs with lymphoma is described. The limitations of the system consisting of an activation of enzymes leading to rapid neosynthesis of asparagine and glutamine are outlined. The possible beneficial effect of future combination therapy with amino acid analogues is discussed.
...
PMID:Successful long-term use of a plasmapheresis reactor system in dogs with lymphoma. 614 36

An ascogenous yeast with high potentialities for L-glutaminase and L-asparaginase formation was isolated from Egyptian soils by the application of the culture enrichment method. The organism, identified as Pichia polymorpha, was obtained through the enrichment of soil samples with a simple medium containing 0.5% L-glutaminase as a major carbon and nitrogen source at low pH values. The amidase activities were produced constitutively on a variety of media irrespective of the presence of their substrates in the growth medium. Assays of enzyme activity have revealed that optimum pH values for L-glutamine and L-asparagine hydrolysis are 6.0 and 6.7, respectively. The L-asparaginase activity of the cells was heat-stable for at least 10 minutes at 60 degrees C. The enzyme exhibited apparent Km of 1.37 x 10(-2) M and 1.95 x 10(-2) M for L-asparagine and L-glutamine, respectively. No metal requirement were detected for the amidase activities of the organism under study.
...
PMID:Formation and properties of L-glutaminase and L-asparaginase activities in Pichia polymorpha. 616 54

In a series of four experiments, asparaginase and glutaminase activity was measured in liver and kidney tissue of 7- to 19-day-old male broiler chicks. In Experiment 1, chicks were fed purified amino acid diets with 14.8 and 44.6% protein equivalents (PE) with 1, 3, or 5% added sodium bicarbonate. In Experiments 2, 3, and 4 the chicks were fed a 23% protein basal control diet, basal diet containing 5% ammonium chloride, and basal diet containing 5% ammonium chloride with 5 or 10% sodium bicarbonate, asparagine, or glutamine. In Experiments 2 and 4 the chicks were also fed 25, 50, or 75% protein-isolated soy-purified diets. The 44.6% PE diet increased liver and kidney asparaginase activity in chicks as compared to chicks fed a 14.8% PE diet. The addition of sodium bicarbonate to the 44.6% PE amino acid diet decreased the kidney asparaginase activity equivalent to kidney asparaginase activity of chicks fed the 14.8% PE diet. Asparaginase activity increased 4-fold in the kidneys of chicks fed the 23% protein basal diet containing 5% ammonium chloride and the pH of the urine from the chicks was 4.9. Chicks fed basal diets with 5% ammonium chloride plus 10% sodium bicarbonate or asparagine had the same kidney asparaginase activity and urine pH as chicks fed the 23% protein basal control diet. Glutamine added to chick diets containing 5% ammonium chloride did not decrease the kidney asparaginase activity or the urine acidity. Liver asparaginase activity was not increased in acidotic chicks fed diets with 5% ammonium chloride. The asparaginase activity of liver and kidney tissue were both significantly increased in chicks fed 75% protein-isolated soy purified diets and the pH of their urine was 5.6. The increase in liver asparaginase of chicks fed 75% protein or 44.5% PE diets was probably due to an endocrine gluconeogenic response producing increased catabolism of the majority of amino acids. The increase in kidney asparaginase of chicks fed 75% protein, 44.5% PE diets, and 23% protein basal diets with 5% ammonium chloride was primarily related to metabolic acidosis. Phosphate-dependent glutaminase (PDG) activity was localized in chick kidney mitochondria and was heat sensitive (55 C for 30 sec). The phosphate-independent glutaminase (PIG) activity was primarily localized in chick kidney mitochondria but was stable to a temperature of 55 C for 30 sec.(ABSTRACT TRUNCATED AT 400 WORDS)
...
PMID:Asparagine and glutamine metabolism in chicks. 632 68

The in vitro blastogenic response of rat splenocytes to concanavalin A stimulation is inhibited by inclusion of asparaginase in the culture medium. The glutaminase-free asparaginase from Vibrio succinogenes is as potent an inhibitor as the Escherichia coli enzyme which has 2% glutaminase activity. The polyethylene glycol-modified forms of both enzymes are also inhibitory. We suggest that previously proposed explanations for the ability of asparaginases to inhibit blastogenesis are not likely to be correct and propose that asparaginase interacts with a mitogenic factor.
...
PMID:Inhibition of blastogenesis by native and polyethylene glycol-modified asparaginases from Escherichia coli and Vibrio succinogenes. 635 Jan 65

The role of glutaminase activity of microbial deamidases in the immunodepressant action of these enzymes was studied. Escherichia coli asparaginase, asparagin and glutamin deamidases from Pseudomonas fluorescens and Mycobacterium album were found to have an inhibitory effect on the PHA-stimulated lymphocyte blast transformation. The inhibitory activity of deamidases with the asparaginase-glutaminase ratios 1 : 1.5 and 1 : 1.3 was one order of magnitude higher than that of Escherichia coli asparaginase with the ratio 1 : 0.02. It is assumed that glutaminase activity plays an essential role in the immunodepressant action of deamidases .
...
PMID:[Comparison of the immunodepressive action of microbial deamidases from different sources]. 642 45

High concentrations of Escherichia coli asparaginase (80 U/ml) altered the binding of concanavalin A (Con A) to L 5178Y murine lymphoma cells that are sensitive to the cytotoxic action of this enzyme. Incubation of the asparaginase sensitive line in asparagine-free media or media containing Acinetobacter glutaminase-asparaginase did not alter the Con A binding of these cells. Escherichia coli asparaginase had no effect on Con A binding of two asparaginase resistant L5178Y cell lines that were isolated and maintained in asparagine depleted or asparaginase containing medium. The E. coli asparaginase preparation inhibited protein and glycoprotein biosynthesis to comparable degrees. It did not have proteolytic or glycolytic activity. Escherichia coli asparaginase did not alter the binding of wheat germ, soybean or ricin agglutinins to any of these cell lines. These data suggest that high concentrations of E. coli asparaginase have a specific effect on the Con A receptor in the sensitive line.
...
PMID:Effect of asparaginase on cell membranes of sensitive and resistant mouse lymphoma cells. 672 17


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---