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:6.3.4.6 (urease)
7,490 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ornithine carbamyl transferase activity was determined by estimation of the citrulline formed during the reaction. Citrulline is estimated by diacetylmonoxime in the presence of thiosemicarbazide. The conditions of enzyme analysis were then studied in buffer veronal-acetate medium at 37 degrees C. The optimum pH for activity depended on the ornithine concentration, but was independent of carbamyl-phosphate concentration. At pH 7.8, ornithine at concentrations higher than 1.6 mM inhibited enzyme activity, ornithine Km was 0.208 mM and that of carbamyl-phosphate was 1.92 mM. The incubation time for determination of OCT activity was 15 minutes. Citrulline production was proportional to the enzyme concentration up to activities of 180 units/l. Serum urea was destroyed by a urease of high quality, so that the formation of citrulline in the control reagents was minimal. Reference values, determined on a hospital population, without liver, heart or pulmonary disease, lay between 4.7 +/- 2.3 units/l. The coefficient of variation of the technique, determined on a pool of serum of moderate activity was 8 units/l i.e. 5.1 per cent.
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PMID:[Determination of the activity of serum ornithine carbamoyltranferase : working conditions in a veronal-acetate medium]. 0 89

Filled hollow fibers were prepared and evaluated for application in hemosorption. Powdered activated carbon, urease-carbon, and macroporous ion exchange resins were used as fillers in highly permeable cellulose acetate hollow fibers. The carbon-filled hollow fibers had better mass transfer properties than encapsulated carbon in solid form. Zirconium phosphate and 2 synthetic zeolites were tested for ammonium ion adsorption from buffered saline and Ringer's salt solutions. Synthetic zeolites were found to have higher specificity and capacity for ammonium ion adsorption than zirconium phosphate. Projections are that hemosorption devices utilizing urease, carbon, and zeolites could remove all nitrogenous waste metabolites currently being treated only by dialysis. Oxystarch and oxystarch derivatives were tested for direct urea adsorption and were found unsuitable for this application.
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PMID:Sorbent-filled hollow fibers for hemopurification. 71 87

Children with inborn errors of urea synthesis who survive neonatal hyperammonemic coma commonly exhibit cognitive deficits and neurologic abnormalities. Yet, there is evidence that ammonia is not the only neurotoxin. Hyperammonemia appears to induce a number of neurochemical alterations. In rodent models of hyperammonemia, uptake of L-tryptophan into brain is increased. It has been reported that in an experimental rat model of hepatic encephalopathy, in the ammonium acetate-injected rat, and in patients with hepatic failure and inborn errors of ammonia metabolism, quinolinate, a tryptophan metabolite, is increased. Elevations in quinolinate are of particular concern, as quinolinate could excessively activate the N-methyl-D-aspartate subclass of excitatory amino acid receptors, thereby causing selective neuronal necrosis. We sought to identify an animal model that would replicate the increases in quinolinate that have been associated with hyperammonemia in humans. Levels of quinolinate were measured in hyperammonemic urease-infused rats and ammonium acetate-injected rats. In the urease-infused rat, brain tryptophan was doubled, and serotonin and its metabolite 5-hydroxyindoleacetic acid were significantly increased. Yet, despite the increase in tryptophan and evidence for increased metabolism of tryptophan to serotonin, there were no observed increases of quinolinate in brain, cerebrospinal fluid, or plasma. In the ammonium acetate-injected rat, significant increases of 5-hydroxyindoleacetic acid in cerebral cortex were also observed, but quinolinate did not change in cerebrospinal fluid or cerebral cortex. In summary, we were unable to demonstrate an increase of quinolinate in brain or cerebrospinal fluid in these rat models of hyperammonemia.
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PMID:Quinolinate in brain and cerebrospinal fluid in rat models of congenital hyperammonemia. 127 10

As part of the development of disposable urea bioselective probes, the covalent binding of urease on ammonium-selective potentiometric membranes has been assessed. Nonactin/bis(1-butylpentyl)adipate/poly(vinylchloride) (PVC) membranes, directly applied to an internal solid contact (conductive epoxy-graphite composite), has been used as a support for covalent immobilization of urease. Two types of all-solid-state construction process have been assayed: thin layers of cellulose acetate (CA) were coated on the PVC ammonium-selective membranes (type 1) and blends of PVC and CA at various ratios were used as ammonium-selective membrane matrices (type 2). Urease was covalently attached to CA via aldehyde groups. These groups were created on the polysaccharide with sodium periodate to which the enzyme was immobilized through a spacer (hexamethylenediamine). The viability of both types of probe for the determination of ammonium ions was assessed after each step of the activation process. Results indicated that type 2 potentiometric probes are altered after the treatment with sodium periodate. Good results were obtained with type 1 probes. Their dynamic concentration range of response to urea was from 2 x 10(-5) to 0.01 M with a sensibility of 50 mV/decade.
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PMID:Covalent binding of urease on ammonium-selective potentiometric membranes. 129 21

Twenty-one type or other reference strains, each representing a different Campylobacter, Helicobacter, or Arcobacter taxon, and a reference strain of Staphylococcus aureus were used to assess the reproducibility of nine enzyme detection tests used in the identification of campylobacters. For five of the tests (alkaline phosphatase, DNase, and H2S production, indoxyl acetate hydrolysis, and nitrate reduction), more than one procedure was employed to determine the most suitable method. Alkaline phosphatase test results were better defined and more reproducible if read after 1 h of incubation. Detection of DNase was fully reproducible with each method (except with Helicobacter pylori), but reactions were generally weaker than those of other DNase-producing organisms. Both procedures for determining H2S production were irreproducible for the same strains. The reproducibility of indoxyl acetate hydrolysis was improved by using disks impregnated with 25 microliters of substrate. Reduction of nitrate was best determined by Cook's plate method. Results for the other tests examined (catalase, oxidase, and urease production and hippurate hydrolysis) were both pertinent and fully reproducible for all strains.
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PMID:Assessment of enzyme detection tests useful in identification of campylobacteria. 155 96

Although successful in reducing urea levels, the use of oral microcapsules containing a urease-silica adduct and a zirconium phosphate ion exchanger result in a number of problems, including a negative calcium balance. In this study, it is demonstrated that the use of microcapsules containing a urease-zeolite preparation may be a potential route to urea removal. The use of zeolite ion exchangers, and zeolite W in particular, can alleviate the problems encountered with zirconium phosphate. Unlike zirconium phosphate, zeolite W is nonselective toward calcium ions and is stable at the high pH found in the intestinal tract. Zeolite W, when present in the sodium form, has a high ammonium capacity of 3.6 mEq NH4+/g zeolite under simulated intestinal conditions; its reactivity to ammonium is also higher. The application of enzyme envelopes to zeolite particles is a novel immobilization procedure that does not involve the use of colloidal silica and can reduce the amount of ingested material by as much as 25%. The current in vitro study shows that cellulose acetate butyrate microcapsules, containing a urease-zeolite preparation, remove up to 80% of urea in less than 1 hour. These microcapsules can be dried and retain activity when sealed in a jar at 4 degrees C.
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PMID:The potential of a microencapsulated urease-zeolite oral sorbent for the removal of urea in uremia. 164 15

Semipermeable nylon-polyethylenimine artificial cells containing leucine dehydrogenase (EC 1.4.1.9), alcohol dehydrogenase (EC 1.1.1.1), urease (EC 3.5.1.5), and dextran-NAD+ were prepared. Artificial cells could convert ammonia or urea into L-leucine, L-valine, and L-isoleucine. For batch conversion in 20.0 mM of ammonium acetate substrate solutions, in 2 h 0.2 ml of artificial cells could produce 4.48 mumol of L-leucine, 9.98 mumol of L-valine, or 5.96 mumol of L-isoleucine. The corresponding conversion ratios were 22.4, 49.9, and 29.8%. In 20.0 mM of urea substrate solutions, 13.71 mumol of L-leucine, 16.12 mumol of L-valine, or 13.44 mumol of L-isoleucine was produced and the conversion ratios were 68.6, 80.6, and 67.2%. The substrate specificity of leucine dehydrogenase for the reductive amination was determined. Of the three branched-chain amino acids produced, the production rates of L-valine were the highest. The apparent Km values were as follows: 0.32 mM for alpha-ketoisocaproate, 1.63 mM for alpha-ketoisovalerate, and 0.73 mM for Dl-alpha-keto-beta-methyl-n-valerate. The leucine dehydrogenase multienzyme system had a good storage stability. It retained 72.0% of the original activity with artificial cells were stored at 4 degrees C for 6 weeks. The optimum conversion pH and temperature were 8.5-9.0 and 35-40 degrees C. The effects of urea and ammonium salts on conversion rate were also studied. The relative activities in ammonium salts solutions were 45.1-75.9% of those in urea solutions.
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PMID:Conversion of ammonia or urea into essential amino acids, L-leucine, L-valine, and L-isoleucine, using artificial cells containing an immobilized multienzyme system and dextran-NAD+. 2. Yeast alcohol dehydrogenase for coenzyme recycling. 169 39

1. Portacaval shunting in rats results in several metabolic alterations similar to those seen in patients with hepatic encephalopathy. The characteristic changes include: (a) diminution of cerebral function; (b) raised plasma ammonia and brain glutamine levels; (c) increased neutral amino acid transport across the blood-brain barrier; (d) altered brain and plasma amino acid levels; and (e) changes in brain neurotransmitter content. The aetiology of these abnormalities remains unknown. 2. To study the degree to which ammonia could be responsible, rats were made hyperammonaemic by administering 40 units of urease/kg body weight every 12 h and killing the rats 48 h after the first injection. 3. The changes observed in the urease-treated rats were: (a) whole-brain glucose use was significantly depressed, whereas the levels of high-energy phosphates remained unchanged; (b) the permeability of the blood-brain to barrier to two large neutral amino acids, tryptophan and leucine, was increased; (c) blood-brain barrier integrity was maintained, as indicated by the unchanged permeability-to-surface-area product for acetate; (d) plasma and brain amino acid concentrations were altered; and (e) dopamine, 5-hydroxytryptamine (serotonin) and noradrenaline levels in brain were unchanged, but 5-hydroxyindoleacetic acid (5-HIAA), a metabolite of 5-hydroxytryptamine, was elevated. 4. The depressed brain glucose use, increased tryptophan permeability-to-surface-area product, elevated brain tryptophan content and rise in the level of cerebral 5-HIAA were closely correlated with the observed rise in brain glutamine content. 5. These results suggest that many of the metabolic alterations seen in rats with portacaval shunts could be due to elevated ammonia levels. Furthermore, the synthesis or accumulation of glutamine may be closely linked to cerebral dysfunction in hyperammonaemia.
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PMID:Hyperammonaemia causes many of the changes found after portacaval shunting. 170 23

A biochemical, physiological and enzymatic study of 78 C. pylori strains isolated from gastroduodenal biopsies is reported. All strains were positive in the oxidase, catalase and urease tests. 97.4% produced SH2 in the lead acetate band and 79.4% showed beta-hemolytic activity in sheep blood agar. In the antibiotic selection tests, C. pylori was characterized to be resistant to nalidixic acid and sensitive to cefalotin . The enzymatic study demonstrated the presence of acid and alkaline phosphatases. This finding and the urease test give C. pylori a define bacteriological character which differentiate it from the remaining campylobacteria.
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PMID:[Biochemical, physiological, and enzymatic study of 78 strains of Helicobacter (Campylobacter) pylori isolated from gastroduodenal biopsies]. 209 88

Reports indicate that L-carnitine administration before 100% lethal dose of ammonium acetate suppresses the symptoms of ammonia toxicity and prevents death in mice. However, we have been unable to confirm this observation. The cause of discrepancy between our results and the results of others was investigated with two models of hyperammonemia in mice: 1) that induced by intraperitoneal injection of urease and 2) that induced by intraperitoneal injection of ammonium acetate. L-Carnitine administration failed to protect mice against ammonia toxicity induced by intraperitoneal injection of urease. Mortality in mice treated with L-carnitine 30 min before injection of ammonium acetate was similar to that of controls pretreated with saline. Ammonia and urea levels in plasma, liver, and brain were also similar in both groups. However, the values were significantly lower than those in mice denied either pretreatment before the ammonium acetate challenge. These results indicate that pretreatment acts to reduce blood and tissue ammonia simply by diminishing the rate of absorption of the challenge, owing to the dilution of ammonium acetate upon mixing with the contents of the peritoneal cavity. Thus, any protocol that does not compare results of a putative protective agent with those obtained with an equal volume of solvents or saline runs the risk of ascribing protective property to the agent when the protection may, in fact, have been afforded by the solvent.
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PMID:Failure of L-carnitine to protect mice against hyperammonemia induced by ammonium acetate or urease injection. 223 23


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