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

Struvite crystals were produced by Proteus mirabilis growth in artificial urine, in the presence of a number of naturally occurring crystallization inhibitors. The use of phase contrast light microscopy enabled the effects of added chondroitin sulfate A, chondroitin sulfate C, heparin sulfate, or sodium citrate, on struvite crystal growth rates to be rapidly monitored as changes in crystal habit. Struvite crystals formed as a consequence of the urease activity of P. mirabilis under all chemical conditions. In the absence of inhibitor, early crystal development was marked by large quantities of amorphous precipitate, followed immediately by the appearance of rapidly growing X-shaped or planar crystals. Addition of the glycosaminoglycans, chondroitin sulfate A, chondroitin sulfate C, or heparin sulfate to the artificial urine mixture had no effect on the rate of crystal growth or appearance. When sodium citrate was present in elevated concentrations, crystal appearance was generally slowed, and the crystals assumed an octahedral, slow growing appearance. None of the added compounds had any influence on bacterial viability, pH, or urease activity. It is therefore likely that the inhibitory activity displayed by sodium citrate might be related to its ability to complex magnesium or to interfere with the crystal structure during struvite formation. From these experiments it would appear that citrate may be a factor in the natural resistance of whole urine to struvite crystallization.
...
PMID:Influence of chondroitin sulfate, heparin sulfate, and citrate on Proteus mirabilis-induced struvite crystallization in vitro. 212 9

When leprosy bacilli grown in nude mouse foot pad were used for culture experiments, cultivable acid-fast bacillus was sometimes isolated as a contaminant. Whenever bacilli were inoculated to nude mice, the same leprosy bacilli were killed by autoclaving and were inoculated in to foot pads of 5 nude mice for examination of this cause of the contamination. Acid-fast bacillus was cultivated on 3% Ogawa egg medium at 33 degrees C from homogenates of foot pads of nude mice infected with M. leprae after one year and a while of infection. Foot pad of nude mouse injected with leprosy bacilli was cut off, ground in mortar and passed through sterile absorbent cotton and the filtrate was centrifuged at 10,000 rpm for 30 minutes. The sediment was inoculated on 3% Ogawa egg medium after treating with a small amount of sterile 1 N sodium hydroxide. Acid-fast bacilli were isolated from 3 out of 41 mice inoculoted with heat killed bacilli. The isolated acid-fast bacillus did not be observed in the same experimental group inocudated with live bacilli, positive cases were scattered in another groups. Four out of 16 tubes were positive for acid-fast bacilli in mice infected with Kurume-naha and 5 out of 7 tubes in the Amami-KM infected mouse group. The two negative tubes were discarded due to contamination. Kurume-Oki strain which has yellow colonial morphology was isolated from one out of 6 culture tubes. Strains Kurume-naha and Amami-KM have the same characteristics as follows: slow grower with pale yellow smooth colonial morphology, strongly positive for niacin production and ureas; positive for nicotinamidase, pyradinamidase and 68 degrees C catalase; no growth at 45 degrees C, negative for nitrate reduction, hydrolysis of Tween 80, diamine oxidase, heat stable acid-phosphatase and arylsulphatase; resistant to streptomycin, isoniazid, rifampicin and B 663. Two isolates were identified as Mycobacterium simiae from these characteristics. Characteristics of a Kurume-Oki isolate was as follows: slow grower with yellow smooth colonial morphology, positive for urease, 68 degrees C catalase, hydrolysis of Tween 80 and arylsulfatase; no growth at 45 degrees C, negative for niacin production, nicotinamidase, pyradinamidase, nitrate reduction, daimine oxidase and heat stable acid-phosphatase; resistant to streptomycin, isoniazid, rifampicin and B. 663. This bacillus was identified as Mycobacterium gordonae from these characteristics.(ABSTRACT TRUNCATED AT 400 WORDS)
...
PMID:[Acid-fast bacilli isolated from foot pads of nude mice infected with leprosy bacilli]. 213 33

We describe a new stable isotope technique for the in vivo study of hepatic plasma protein synthesis in humans. The method involves the infusion of (13C)sodium bicarbonate for 1 h and the measurement of the isotopic enrichment of (13C)arginine in newly synthesized apolipoprotein B of very low density lipoproteins (VLDL-apoB) and low density lipoproteins (LDL-apoB) in blood samples taken over a 5-6 h period from the commencement of the infusion. Isotope ratio mass spectrometry was utilized to measure 13CO2 enrichment following hydrolysis of these proteins and conversion of the guanidinium carbon of arginine in the hydrolysate to carbon dioxide by sequential incubation with arginase and urease. The method is capable of measuring isotopic enrichment as low as 0.001 at.% excess (APE) with a precision of 1.2%. In both subjects studied, the (13C)arginine of VLDL-apoB reached enrichments of 0.2 APE and that of the arginine of LDL-apoB, 0.03 APE. Incorporation of labeled arginine into LDL-apoB was demonstrable at 60-90 min. The new technique is safe and is applicable to the study of the hepatic biosynthesis of a wide range of plasma proteins.
...
PMID:Measurement of (C13)arginine incorporation into apolipoprotein B-100 in very low density lipoproteins and low density lipoproteins in normal subjects using (13C)sodium bicarbonate infusion and isotope ratio mass spectrometry. 216 33

Urease of Helicobacter pylori (formerly Campylobacter pylori) is believed to represent a critical virulence determinant for this species. Ammonia generated by hydrolysis of urea may protect the acid-sensitive bacterium as it colonizes human gastric mucosa. An H. pylori strain, cultured from a gastric biopsy of a patient with complaints of abdominal pain and a history of peptic ulcer disease, was isolated on selective medium and cultured in Mueller-Hinton broth supplemented with 4% fetal calf serum. Whole cells were ruptured by French pressure cell lysis, and soluble protein was chromatographed on DEAE-Sepharose, phenyl-Sepharose, Mono-Q, and Superose 6 resins. Purified urease represented 6% of the soluble protein of crude extract, was estimated to have a native molecular size of 550 kilodaltons (kDa), and was composed of two distinct subunits of apparent molecular sizes of 66 and 29.5 kDa. On the basis of subunit size, a 1:1 subunit ratio as measured by scanning densitometry of Coomassie blue-stained sodium dodecyl sulfate-polyacrylamide gels, and estimated native molecular size, the data are consistent with a stoichiometry of (29.5 kDa-66 kDa)6 for the structure of the native enzyme. Km for urea was estimated at 0.2 mM. By N-terminal analysis, the 29.5-kDa subunit of H. pylori urease was found to share significant amino acid sequence similarity with the smallest of three subunits of the Proteus mirabilis and Morganella morganii ureases, as well as to the amino terminus of the unique jack bean subunit. The 66-kDa subunit also shared up to 80% similarity with the largest of three subunits of P. mirabilis, M. morganii, and Klebsiella aerogenes ureases and to internal sequences (amino acids 271 to 285) of the jack bean urease subunit. Thus, the amino acid sequence is conserved among ureases with one, two, and three distinct subunits, suggesting a common ancestral urease gene. Also, urease subunits of M. morganii and jack bean were specifically recognized by antisera raised against the 66-kDa subunit of H. pylori urease, demonstrating that at least some antigenic determinants were conserved among ureases from different species.
...
PMID:Purification and N-terminal analysis of urease from Helicobacter pylori. 231 39

A method for the simultaneous determination of hypotaurine and taurine was developed. The method consisted of the elimination of urea, which interfered with the determination of hypotaurine, by immobilized urease, and determination of hypotaurine and taurine with an amino acid analyzer. The analyzer equipped with a cation-exchange column was operated at 32 degrees C with 0.2 M sodium citrate buffer, pH 2.8. Using this method, the dynamics of hypotaurine and taurine in blood plasma of rats was studied after the intraperitoneal injection of L-cysteine. The concentration of cysteine reached the maximum 1 h after L-cysteine loading. The concentration of hypotaurine and taurine increased in parallel and reached the maximum 2 h after L-cysteine loading. These changes seem to indicate the precursor-product relationship of these substances and the rapid conversion of hypotaurine to taurine in vivo.
...
PMID:Determination of hypotaurine and taurine in blood plasma of rats after the administration of L-cysteine. 233 Aug 45

Sonication of Ureaplasma urealyticum cells grown in a dialysate growth medium effectively separated the cytoplasmic fraction from the membrane fraction, with both fractions relatively free from exogenous contaminating proteins. The urease activity was associated with the cytoplasmic fraction, and the ureaplasmal urease exhibited a specific activity higher than that of crystalline jack bean urease. The enzymatic activity of the ureaplasmal enzyme was optimum at pH 7.5 and was resistant to the chelating agents EDTA and sodium citrate. Sulfhydryl-blocking agents such as HgCl2 and Pb(NO3)2 inhibited the ureaplasmal urease, which was also shown to be particularly sensitive to flurofamide and, to a much lesser extent, to acetohydroxamic acid. Electrophoretic analysis of the proteins of the ureaplasmal cell fractions combined with Western immunoblot with an antiserum to the ureaplasmal urease indicated that the urease constitutes a major component of the cytoplasm and is composed of several 70-kilodalton polypeptides.
...
PMID:Characteristics of Ureaplasma urealyticum urease. 313 6

Since sodium benzoate, which is widely used to treat hyperammonemia its effect on mitochondrial urea cycle enzymes was investigated. its effect on mitochondrial urea cycle enzymes was investigated. Sodium benzoate was administered to urease treated hyperammonemic rats and controls. In both groups no interference with the activity of carbamylphosphate synthetase, ornithine carbamyltransferase and N-acetylglutamate synthetase in the liver could be observed at concentrations of benzoate in plasma found in hyperammonemic patients. Careful monitoring of plasma levels reduces benzoate toxicity as shown in a patient with argininosuccinic aciduria.
...
PMID:Mitochondrial urea cycle enzymes in rats treated with sodium benzoate. 334 18

Campylobacter pylori, a suspected agent of gastritis and peptic ulceration, rapidly hydrolyzes urea. Because urease serves as the basis of detection of the organism in gastric biopsies and may represent an important virulence factor, biochemical characteristics of the enzyme were determined. C. pylori was isolated from antral biopsies from 10 patients with complaints of abdominal pain or history of peptic ulcer disease. All isolates were urease positive, with an average rate of hydrolysis by cell lysates being 36 +/- 28 mumol of NH3 per min per mg of protein, more than twice that of Proteus mirabilis and 10 times that of other urinary tract isolates. The enzyme had an apparent molecular weight of 625,000 +/- 15,000 by column chromatography, an isoelectric point of 5.9, a Km of 0.8 +/- 0.1 mM urea, an optimal temperature of 45 degrees C, and an optimal pH of 8.2. Ten isolates tested produced ureases with identical electrophoretic mobilities on nondenaturing 5% polyacrylamide activity gels. Acetohydroxamic acid (100 micrograms/ml), hydroxyurea (85 micrograms/ml), flurofamide (0.05 micrograms/ml), and EDTA (8 mM) inhibited enzyme activity by 50%. Cell lysates retained 50% of initial urease activity after 6 days and 40% activity after 18 days when stored at 4 degrees C in 20 mM sodium phosphate, pH 6.8. At -70 degrees C for 18 days, 1 mM EDTA or 15% glycerol preserved 40 or 34%, respectively, of initial activity. The urease of C. pylori appears to be biochemically unique from the enzymes of other common urease-producing species.
...
PMID:Characterization of urease from Campylobacter pylori. 338 8

Proteus mirabilis, a gram-negative bacillus, is often implicated in the formation of infectious kidney stones. As ureolytic activity of this organism is thought to play a major role in its pathogenesis, we adapted our recently described urease localization technique to visualize urease activity in vivo. Urease activity was ultrastructurally localized in two clinically isolated P. mirabilis strains by precipitating the enzymatic reaction product (ammonia) with sodium tetraphenylboron. Subsequent silver staining of the cells revealed urease activity to be predominantly associated with the periplasm and outer membranes of each strain. Biochemical measurements of urease activity in P. mirabilis cell fractions correlated well with histochemical observations in that the majority of urease activity was associated with the periplasm. Membrane-bound urease activity of these strains was associated mainly with the peptidoglycan in the detergent-insoluble (outer membrane) fraction.
...
PMID:Histochemical and biochemical urease localization in the periplasm and outer membrane of two Proteus mirabilis strains. 353 91

Klebsiella aerogenes urease was purified 1,070-fold with a 25% yield by a simple procedure involving DEAE-Sepharose, phenyl-Sepharose, Mono Q, and Superose 6 chromatographies. The enzyme preparation was comprised of three polypeptides with estimated Mr = 72,000, 11,000, and 9,000 in a alpha 2 beta 4 gamma 4 quaternary structure. The three components remained associated during native gel electrophoresis, Mono Q chromatography, and Superose 6 chromatography despite the presence of thiols, glycols, detergents, and varied buffer conditions. The apparent compositional complexity of K. aerogenes urease contrasts with the simple well-characterized homohexameric structure for jack bean urease (Dixon, N. E., Hinds, J. A., Fihelly, A. K., Gazzola, C., Winzor, D. J., Blakeley, R. L., and Zerner, B. (1980) Can. J. Biochem. 58, 1323-1334); however, heteromeric subunit compositions were also observed for the enzymes from Proteus mirabilis, Sporosarcina ureae, and Selemonomas ruminantium. K. aerogenes urease exhibited a Km for urea of 2.8 +/- 0.6 mM and a Vmax of 2,800 +/- 200 mumol of urea min-1 mg-1 at 37 degrees C in 25 mM N-2-hydroxyethylpiperazineN'-2-ethanesulfonic acid, 5.0 mM EDTA buffer, pH 7.75. The enzyme activity was stable in 1% sodium dodecyl sulfate, 5% Triton X-100, 1 M KCl, and over a pH range from 5 to 10.5, with maximum activity observed at pH 7.75. Two active site groups were defined by their pKa values of 6.55 and 8.85. The amino acid composition of K. aerogenes urease more closely resembled that for the enzyme from Brevibacter ammoniagenes (Nakano, H., Takenishi, S., and Watanabe, Y. (1984) Agric. Biol. Chem. 48, 1495-1502) than those for plant ureases. Atomic absorption analysis was used to establish the presence of 2.1 +/- 0.3 mol of nickel per mol of 72,000-dalton subunit in K. aerogenes urease.
...
PMID:Purification and characterization of the nickel-containing multicomponent urease from Klebsiella aerogenes. 355 84


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

---