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)

Fast protein liquid chromatography and SDS-PAGE have been used to isolate and purify Helicobacter pylori urease. A nickel component of the urease was detected in the purified proteins by atomic absorption spectroscopy. The nickel was present only in the 61 kDa polypeptide and in the ratio of between five and six atoms to one molecule of urease, suggesting a hexameric structure. These results are discussed in relation to other bacterial ureases and urease activity at low pH.
...
PMID:The demonstration of nickel in the urease of Helicobacter pylori by atomic absorption spectroscopy. 200 97

The urease from Ureaplasma urealyticum (serotype 8) has been purified by immuno-affinity column chromatography. Two active nickel-containing forms of the enzyme were demonstrated by non-denaturing electrophoretic analysis and a single active peak of apparent molecular mass 190 kDa was shown by FPLC. Total inactivation and denaturation of the enzyme to give three subunit polypeptides (one of 72 kDa containing nickel, one of 14 kDa and one of 11 kDa) was achieved by treatment with SDS and boiling. Densitometry suggested that the active enzyme contains equimolar ratios of the three subunits and hence is a hexamer. The enzyme displayed a pH optimum of 6.9 and pI values were determined. Storage of the purified enzyme at -70 degrees C followed by thawing to 20 degrees C caused a partial breakdown to inactive subunits. Anti-urease monoclonal antibodies bound both to the active enzyme and to the inactive 72 kDa subunit, and the antibodies cross-reacted with ureases from all of the other human serotypes. Competition assays with the antibodies revealed four distinct epitopes of the enzyme, all distinct from its active site.
...
PMID:The urease of Ureaplasma urealyticum. 248 31

Jack bean (Canivalia ensiformis) urease (EC3.5.1.5) was purified in one-step by ligand affinity chromatography using epoxy-activated Sepharose 6B-urea. The yield of the purified enzyme was about 80% with a specific activity of about 500 U/mg of protein. The enzyme was apparently homogeneous when analyzed by SDS-PAGE and native PAGE. The protein band on native PAGE coincided with the stained band of urease activity. The affinity column could be regenerated and reused several times without any loss of binding capacity and resolution. Affinity gels containing either acetamide or semicarbazide as affinity ligands were also found to be useful for the isolation of urease.
...
PMID:One-step affinity purification of urease from jack beans. 314 23

The urease enzyme of Campylobacter pylori was studied and compared with that of a related spiral-shaped bacterium, St1, isolated from the rodent ileum. Both bacteria possessed constitutive urease enzymes with activities up to 20-70 times that of Proteus vulgaris. This activity was retained on SDS-polyacrylamide gels. A major catalytic subunit of mol. wt 300,000 was located for all (six) strains of C. pylori subjected to SDS-PAGE whereas St1 had two active forms of mol. wts 140,000 and 150,000. Western-blot analysis indicated the presence of anti-urease antibodies in the sera of patients with C. pylori-associated gastritis. The response to C. pylori urease was not strain-specific but no cross-reactivity was detected between the C. pylori enzyme and that of St1. The very high urease activity of these bacteria is likely to be important in colonisation of the host. Possession of glutamate dehydrogenase activity by both organisms suggests that one role of the urease may be to assimilate the available urea nitrogen. Modification of the local environment to facilitate long-term colonisation is another possible function. Protection from acid is unlikely to be a primary role as the natural habitat of the organism St1 is the non-acid-secreting tissue of the small intestine.
...
PMID:The urease enzymes of Campylobacter pylori and a related bacterium. 317 69

The urease from Ureaplasma urealyticum strain T 960 was isolated by the use of affinity chromatography, hydrophobic chromatography and gel filtration. The enzyme was purified by a factor of 155. The urease appeared as a single band of molecular weight (MW) 75,000 using reducing conditions in SDS-polyacrylamide gel electrophoresis. By gel filtration the native MW was determined to be 150,000. Isoelectric focusing showed the presence of two closely migrating enzyme species with a pI of pH 5.1-5.2. These findings show multiple forms of the urease and that these forms are composed of subunits. The electrophoresis experiments also indicate that this enzyme is a major component of the cytoplasm of U. urealyticum. The Km of the purified enzyme was 4.5 mM urea and the specific activity was 33530 mumoles NH3 x min-1 x mg-1. The optimum pH was pH 7-7.5. The urease activity was inhibited by flurofamide, acetohydroxamic acid, N-ethylmaleimide and p-chloromercuribenzoate but not by iodoacetate.
...
PMID:Purification and characterization of urease from Ureaplasma urealyticum. 319 54

Twenty-one strains comprising Campylobacter laridis (nine), nalidixic acid sensitive campylobacters (NASC) (four), and urease-positive thermophilic campylobacters (UPTC) (eight) were characterized by one-dimensional SDS-PAGE of cellular proteins. The UPTC and NASC strains included six from river water, two from mussels and four from sea water. The type strains of three other Campylobacter species were included for reference. The protein patterns, which contained 45-50 discrete bands, were highly reproducible and were used as the basis for two numerical analyses. In the first, which included all the protein bands, the 21 strains formed nine clusters at the 80% similarity (S) level. The typical C. laridis strains were restricted to two phenons (2 and 5); the atypical strains being distributed among the remaining phenons. In the second analysis, which excluded the principal protein bands (40-48.5 kD range), the 21 strains formed five clusters at the 80% S level. The typical C. laridis strains were relatively homogeneous and fell into a single phenon (2) within which two subgroups were discernable. The atypical strains were more heterogeneous with respect to background protein pattern, with representatives appearing in all five phenons. An electropherotyping scheme comprising six electropherotypes, and based on both analyses is proposed. The high within-group S level and separation from reference strains of Campylobacter in the second analysis, suggested that UPTC and NASC strains belonged within C. laridis possibly as biovars.
...
PMID:Numerical analysis of electrophoretic protein patterns of Campylobacter laridis and allied thermophilic campylobacters from the natural environment. 320 18

Analysis by SDS-PAGE of Ureaplasma urealyticum (predominantly serotype 8), propagated in a growth medium containing 10% (v/v) foetal calf serum, revealed a complex series of polypeptides apparently free of medium contaminants. Serological analysis using an immobilized antibody reagent, and immunoblotting using a polyclonal serum, showed the presence of two major and several minor antigens. One major antigen, a putative surface component of apparent molecular mass 96 kDa was shown, with a monoclonal antibody, to be serotype-specific. Growth of the organism was partially suppressed in the presence of the antibody. The second major antigen had an apparent molecular mass of 76 kDa and was presumed to be an internal component since it failed to label with the Bolton and Hunter reagent, in contrast to the 96 kDa antigen. Another monoclonal antibody was characterized which detected the canonical urease enzyme of the organism serotype 8 and of the two other human serotypes tested. Purification of this urease antigen by affinity chromatography and electrophoretic analysis of polypeptides after denaturation revealed a single polypeptide of molecular mass 76 kDa, putatively related to the above major antigen. Enzymic activity could be recovered after purification and demonstrated by in situ techniques only when electrophoretic analysis was done under non-denaturing conditions suggesting that the functional enzyme is a multimeric complex.
...
PMID:Preliminary characterization of the urease and a 96 kDa surface-expressed polypeptide of Ureaplasma urealyticum. 344 56

We have purified urease from the Mollicutes, Ureaplasma urealyticum, using high performance liquid chromatography methods and DEAE-Sephadex chromatography. While only small amounts of material could be utilized in these methods, urease was purified at least 180-fold, yield a major band on SDS-PAGE of 66,000 daltons, a minor band of 64,000 daltons, and several faint bands of lower molecular mass. These results suggest that the 380,000 dalton intact urease is a pentamer or hexamer of these two larger subunits. The highly purified urease from DEAE-Sephadex retained full activity for at least 20 days at 4 degrees C in sodium phosphate buffer (pH 7.2) with 1% bovine serum albumin. The estimated specific activity of the DEAE peak fractions, 180 IU/micrograms, is at least 90-fold greater than that of jack bean urease.
...
PMID:Purification of urease from Ureaplasma urealyticum. 369 Apr 18

Urease from Bacillus pasteurii DSM 33 was purified 34-fold to a maximum specific activity of 996.5 mumol urea min-1 mg-1 at 30 degrees C. Homogeneity was demonstrated by isoelectric focussing which showed a single protein zone corresponding to a pI of about 4.6. The native enzyme was demonstrated to have a molecular mass of 230,000 and to consist of identical subunits of 65,500, as measured by SDS electrophoresis. Radioactive 63Ni-nickel co-chromatographed with urease through gel filtration, ion-exchange, and affinity chromatography. Measuring specific radioactivity, the nickel content was found to be 1.00 (+/- 0.1) g-atom Ni per mol of subunit, and 0.82 g-atom Ni per mol as measured by atomic absorption spectrometry. This indicates that 1 atom of nickel is present in each of four subunits of the enzyme.
...
PMID:Nickel-content of urease from Bacillus pasteurii. 375 42

HP-specific antibodies were measured in each collected fraction obtained from gel-filtrated separation method with selected patients sera by enzyme-linked immunosorbent assay (ELISA). Most of the fractions reacted with the patients sera also responded to HP urease-specific monoclonal antibodies. In addition, the fractions which showed urease activity strongly correlated with the HP antibody positive ones. Also, we could not detect any cross-reactivity to ureases of other species. Moreover, most patient sera strongly responded to the purified HP urease B subunit separated with SDS/PAGE by western blotting analysis. These findings suggest that the major target for HP-specific antibodies appears to be HP-urease, in particular around 68kd large molecule, urease B subunit and such urease-specific antibodies are isolate-species specific.
...
PMID:[Analysis of immune response to Helicobacter pylori--identification of the protein recognized by anti-Helicobacter pylori antibodies from sera of patients with gastroduodenal diseases]. 783 86


1 2 3 4 5 6 Next >>

---