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)

A urease-antibody conjugate was used in an enzyme-linked immunoassay (ELISA) for the detection of antibodies in blastomycosis. A Blastomyces dermatitidis immunodiffusion antigen was used as the reference antigen in a solid phase indirect ELISA procedure and the endpoints were determined visually. Urease ELISA results on serum specimens from patients with blastomycosis compared favorably (90%) with results obtained spectrophotometrically by the alkaline phosphatase enzyme system. Specificity was evaluated with assays on sera from patients with histoplasmosis (20% cross reactivity), coccidioidomycosis (0% cross reactivity) and on Histoplasma capsulatum skin-test positive individuals (0% cross reactivity). The ease of performance of the urease ELISA combined with no requirements for specialized spectrophometric equipment are factors that favor the continued development of the test as an alternative serodiagnostic method. The assay may prove to be useful and a valuable adjunct to fungal antibody screening procedures.
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PMID:Use of a urease-antibody conjugate in an enzyme immunoassay for the detection of blastomycosis. 366 59

Benzoyl- and isopentenoyl phosphoric triamides (BPA and IPA) strongly inhibited urease activities from jack bean, soybean, watermelon seed, Proteus mirabilis, P. rettgeri, P. vulgaris, Mycobacterium smegmatis, and Ureaplasma urealyticum. Their I50 values (the final concentration causing 50% inhibition), independent of enzyme source, were 2-21 nM, which are about 1,000-fold lower than that of caprylohydroxamic acid, one of the most potent urease inhibitors. ATP-urea amidolyase activity was inhibited 50% by BPA at a higher concentration of 0.28 mM, but was not affected by IPA even at 1.3 mM. Thirteen kinds of hydrolases (trypsin, chymotrypsin, thermolysin, leucine aminopeptidase, papain, lipase, alpha-amylase, glucuronidase, asparaginase, arylsulfatase, alkaline phosphatase, acid phosphatase, and true cholinesterase), two oxidoreductases (catalase and alcohol dehydrogenase), three transferases (glutamic-oxaloacetic aminotransferase, gamma-glutamyl transpeptidase, and arylsulfotransferase) and two kinases (pyruvate kinase and creatine kinase) were not affected at all even at 1 mM BPA and IPA. Exceptionally, pseudo-cholinesterase from human serum was inhibited by BPA and IPA, whose I50 values were 70 nM and 10 muM, respectively, using acetylthiocholine as a substrate. These values increased to 0.55 muM and 54 muM, respectively, when acetylcholine was used as a substrate. These results show that N-acylphosphoric triamides potently and specifically inhibit urease activity at concentrations of nM order.
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PMID:Specific inhibition of urease by N-acylphosphoric triamides. 384 42

The calculolytic effect of a diet designed to reduce the urine concentration of urea, P, and Mg was evaluated in female Beagles with induced urease-positive urinary tract infections and struvite urolithiasis and in female Beagles with induced sterile struvite urolithiasis. The reduced-protein calculolytic diet induced urolith dissolution in 5 of 6 infected dogs with struvite urolithiasis in 2 to 5 months (means = 14.4 weeks). At the end of 6 months, uroliths in comparable control dogs fed a maintenance diet were 5 times larger and 14 times heavier than at the beginning of the study. The calculolytic diet induced urolith dissolution in 6 of 6 noninfected dogs with struvite uroliths in 2 to 4 weeks (means = 3.3 weeks). Four uroliths in noninfected dogs fed the maintenance diet dissolved over a period of 2 to 5 months (means = 14 weeks). Urolith dissolution in dogs fed the calculolytic diet was associated with diet-induced diuresis, reduction in urine pH, reduction in urine concentration of urea ammonia, P, and Mg, and increase in urine titratable acidity. Consumption of the calculolytic diet was also associated with significant (P = less than 0.01) reduction in the serum concentration of urea and albumin and a significant (P = less than 0.01) increase in serum hepatic alkaline phosphatase activity. Concomitant occurrence of hydropic degeneration of hepatocytes indicated that these biochemical and morphologic changes were associated with dietary protein restriction.
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PMID:Evaluation of a calculolytic diet in female dogs with induced struvite urolithiasis. 647 63

Day-old pigs were individually fed a low nickel (0.16 ppm) liquid milk-based diet supplemented with either 0, 5 or 25 ppm nickel on a dry matter basis for a 21-day period. At the end of the liquid feeding period, five pigs per treatment were killed, and the remaining five were fed a dried skim milk-based diet (0.12 ppm nickel) with similar levels of added nickel for an additional 28 days. Dietary nickel did not affect animal gain, liver cholesterol, serum protein concentrations or bacterial urease activity in the gastrointestinal tract. The addition of 5 ppm nickel to the basal dry diet reduced ammonia concentrations in the cecum by 33%. Pigs receiving the high level of nickel had decreased serum alkaline phosphatase and increased serum glucose at 49 days, compared to controls. Animals receiving 5 ppm nickel had higher liver iron and zinc concentrations than controls at 21 days but not at 49 days. Control pigs had lower kidney and lung nickel concentrations than animals receiving 5 ppm nickel at 21 days but not at 49 days. Increasing dietary nickel from 5 to 25 ppm resulted in increased concentrations of nickel in serum, kidney, lung, spleen and muscle. These results suggest that 0.12-0.16 ppm nickel is adequate for growth of neonatal pigs fed milk-based diets. However, additional nickel may improve the iron and zinc status of the young pig.
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PMID:Effect of dietary nickel on growth, urease activity, blood parameters and tissue mineral concentrations in the neonatal pig. 672 54

The API STAPH-IDENT system was compared with conventional methods for the identification of 14 Staphylococcus species. Conventional methods included the Kloos and Schleifer simplified scheme and DNA-DNA hybridization. The API STAPH-IDENT strip utilizes a battery of 10 miniaturized biochemical tests, including alkaline phosphatase, urease, beta-glucosidase, beta-glucuronidase, and beta-galactosidase activity, aerobic acid formation from D-(+)-mannose, D-mannitol, D-(+)-trehalose, and salicin, and utilization of arginine. Reactions of cultures were determined after 5 h of incubation at 35 degrees C. Results indicated a high degree of congruence (greater than 90%) between the expedient API system and conventional methods for most species. The addition of a test for novobiocin susceptibility to the API system increased the accuracy of identification of S. saprophyticus, S. cohnii, and S. hominis, significantly. Several strains of S. hominis, S. haemolyticus, and S. warneri which were difficult to separate with the Kloos and Schleifer simplified scheme were accurately resolved by the API system.
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PMID:Identification of Staphylococcus species with the API STAPH-IDENT system. 675 90

1. A long-term experiment was made with the Rumen Simulation Technique (Rusitec), in which the fermentation of a mixed ration of hay (10 g/d) and bruised barley (5 g/d) was compared with the fermentation of the same diet in the presence of 2, 10 and 50 mg monensin/d. 2. Monensin depressed the production of acetic and butyric acids, markedly increased the production of propionic acid and virtually, eliminated the production of isovaleric acid. The production of methane was decreased in the presence of monensin, but this decrease could be accounted for entirely by the changes in the production of volatile fatty acids and redistribution of metabolic hydrogen. 3. The digestibility of dry matter (DM) in the rations declined in the presence of monensin. Determinations of the rates of digestion showed that the digestion of the readily-fermented food in the initial stages was not affected by monensin, but that at 24 h digestion had been inhibited by monensin. The inhibition was due entirely to its effect on the digestion of the fibrous components. Digestion of non-fibrous material was not affected. 4. The efficiency of microbial growth, expressed as g dry weight/mol ATP formed (YATP) and in terms of DM digested, tended to be increased by monensin. This however occurred only at high, non-practical doses. 5. Urease (EC 3. 5. 1. 5) was induced by the addition of urea of the fermentation, but monensin had no effect on urease activity. Although monensin increased the activity of protease in washed suspensions, more food protein apparently escaped degradation. This may have been due to decreased deaminative activity. 6. Monensin altered the microscopic appearance of the fermentation fluid, and changed the activity of some enzymes in sonicated extracts, including alkaline phosphatase (EC 3. 1. 3. 1), acetate kinase (EC 2. 7. 2. 1) and succinate dehydrogenase (EC 1. 3. 99. 1). These results are discussed in terms of known sensitivities of rumen microbes to monensin and their contribution to the fermentation as a whole.
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PMID:Effect of monensin on the fermentation of basal rations in the Rumen Simulation Technique (Rusitec). 702 Jul 49

1. The Rumen Simulation Technique (Rusitec) was used in a series of long-term experiments to study the distribution and changes of urease (EC 3.5.1.5) activity in a heterogeneous fermentation system. 2. It was shown that in Rusitec the high urease activity from the inoculum decreased to low values, that the rate of decrease was consistent with simple dilution of ureolytic micro-organisms and that the urease activity could be restored to original values by infusion of urea into the reaction vessels. The magnitude of this urease activity was a direct function of the amounts of urea infused. Single daily additions of the same or greater amounts of urea in food or as solid failed to increase the urease activity significantly. 3. In general, urease activity increased 2-6 h after feeding and the increases were greater with roughage diets. 4. The ureolytic activity per unit volume was always higher in compartment 2(space occupied by micro-organisms that are loosely associated with the solid) than in compartment 1 (strained rumen contents) or compartment 3 (space occupied by microbial population that cannot be washed out of the solid matrix). 5. The distribution of urease activity between the compartments was different from the distribution of certain other enzymes (e.g. protease and alkaline phosphatase (EC 3.1.3.1)). 6. Apart from the boundary region, the concentrations of urease, ammonia and volatile fatty acids in compartment 2 were constant, while the concentrations of protein, DNA and another enzyme (alkaline phosphatase) increased with the depth of the compartment. Specific urease activity (per unit weight of protein or DNA) was much higher in compartment 1 than in compartment 2 and it decreased markedly with depth of compartment. 7. The concentrations of ammonia were always much higher in the solid matrix (compartments 2 and 3) than in the free suspension of micro-organisms (compartment 1). There was a linear relation between these two quantities. 8. The results are discussed in relation to published work on the entry and metabolism of urea in the rumen.
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PMID:Distribution and changes in urease (EC 3.5.1.5) activity in Rumen Simulation Technique (Rusitec). 703 70

Previously, nine fecal isolates from wild birds and a domestic swine were identified as helicobacters by phenotypic characterization and reaction with a helicobacter genus-specific DNA probe. These isolates fell into three biotypes by analysis of phenotypic traits. To further characterize these isolates, full 16S rRNA sequences were determined for strains representing each biotype, and sequence comparison indicated that the strains represented three novel, phylogenetically defined Helicobacter species. Three 16S rRNA-based DNA probes were designed and used to identify the remaining strains. Probe reactivity divided the strains into the same three groups identified phenotypically. Six of the isolates represented a new species of the genus Helicobacter for which we propose the name Helicobacter pametensis sp. nov. The following phenotypic features distinguished H. pametensis from other Helicobacter and Campylobacter species: positive tests for oxidase, catalase, alkaline phosphatase, nitrate reduction, growth at 42 degrees C, and growth in the presence of 1% glycine; negative tests for urease, gamma glutamyl transpeptidase, indoxyl acetate hydrolysis, and hippurate hydrolysis; and susceptibility to nalidixic acid and cephalothin. H. pametensis cells were motile and possessed one subterminal sheathed flagellum at each end. The two additional Helicobacter species were similar to H. pametensis except that they were urease positive, hydrolyzed indoxyl acetate, and were resistant to cephalothin. Because these two additional species are phenotypically similar and are represented by only two isolates for one species and one isolate for the other, they are not formally named but are referred to as Helicobacter sp. "Bird-B" and Helicobacter sp. "Bird-C."(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Phylogeny of Helicobacter isolates from bird and swine feces and description of Helicobacter pametensis sp. nov. 752 Jul 43

Beagle serum proteins were separated by polyacrylamide gel electrophoresis (PAGE) and the electrophoretograms were examined by one- and two-dimensional analyses with a laser densitometer. In order from the anodic side of the PAGE pattern, pre-albumin, hexokinase, tyrosinase, alkaline phosphatase, urease, and aldehyde dehydrogenase were assumed to be present based on Rf and Mw. Serum albumin, lactate dehydrogenase, and catalase appeared to be present based on a comparison of their electrophoretic mobility with that of protein standards of known Mw. Verification of beagle serum protein fractions by immunofixation electrophoresis and western blotting electrophoresis, with rabbit anti-human serum, indicated alpha 1-antitrypsin, albumin, haptoglobin, ceruloplasmin, C3c complement, IgG, and IgA. Serum protein fraction values (%) obtained by one- and two-dimensional analyses were similar.
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PMID:Analysis of a polyacrylamide gel electrophoretogram of beagle serum protein by laser densitometer. 765 Sep 2

We analyzed 11 H. pylori isolates from humans using the artificial chromogenic substrate paranitrophenylphosphorylcholine to detect phospholipase C (PLC) activity. The range of PLC in sonicates was 8.8-92.3 (Mean 56.9 +/- 6.5) nmol of substrate hydrolysed min-1 mg-1 protein; the amount of activity was not associated with urease or cytotoxin levels. Addition of sorbitol or glycerol enhanced PLC activity of H. pylori sonicate and purified PLC from C. perfringens (PLC1) but not purified PLC from B. cereus (PLC3). H. pylori sonicates had little acid phosphatase and no detectable alkaline phosphatase activity, and H. pylori PLC showed markedly different biochemical characteristics from either phosphatase. In total, these studies indicate that activity measured in H. pylori sonicate by PLC assay is due to PLC and not phosphatase activity. The temperature optimum for PLC activity of H. pylori sonicate was 56 degrees C and for PLC 1 was 65 degrees C. For H. pylori PLC and PLC1, optimal activity occurred at pH 8. Despite multiple similarities between H. pylori PLC and PLC1, known PLC inhibitors show different interactions with each enzyme. Although PLC activity is present in many subcellular constituents of H. pylori, including culture supernatants and water extracts, highest specific activity is associated with a membrane-enriched fraction.
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PMID:Identification and characterization of Helicobacter pylori phospholipase C activity. 828 Sep 31


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