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)

Urease has been localized in sections of cotyledons from germinating seeds of jack bean, using FITC-labelled immunoglobulin prepared from urease antiserum raised in rabbits. The complication of lectin binding to the immunoglobulins was resolved by treatment of the sections with specific glycosides. Urease is localized in 2 sites: within the cytoplasm of storage parenchyma cells in spherical granules up to 3 micrometer in diameter, and within the intercellular spaces in spherical granules. Although similar in size, the latter are distinguished from the cytoplasmic granules by the presence of beta-lectin and appear to function as an extracellular lytic compartment or lysosome.
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PMID:Immunofluorescent localization of urease in the cotyledons of jack bean, Canavalia ensiformis. 33 36

Helicobacter pylori can be considered a very successful organism effectively colonizing the majority of the world's population. Although various disease states associated with this infection have been described, the mechanisms of pathogenicity remain unknown. The easiest virulence factors to identify are those enabling the organism to colonize the hazardous microenvironment of the gastric epithelium, survive at this site, and multiply sufficiently for transmission to a new host. The factors identified to date include the bacterial enzymes urease and catalase, flagella, and lectin-like adhesins. In addition, it is proposed that the organism has evolved mechanisms to avoid the local antibody responses of the host. Several putative virulence factors that could directly cause gastroduodenal damage have also been identified. These include the direct tissue damage by cytotoxins or the products of urease activity and the indirect tissue damage due to disruption of mucin integrity. Such mechanisms may contribute to peptic ulcer formation; however, the chronic superficial gastritis most frequently associated with this infection is probably caused by immunopathologic events mediated by the host in response to the continued antigen load on the gastric mucosa.
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PMID:Virulence factors of Helicobacter pylori. 177 22

Lectins from the lichen Xanthoria parietina develop arginase activity. One of these lectins behaves as a secreted arginase whereas another is an endocellular enzyme. Both enzymes are glycosylated proteins differing in the occurrence of galactose instead of N-acetyl-D-glucosamine in secreted arginase. The affinity for the algal ligand (glycosylated cell wall urease) of secreted arginase is higher than that shown for the endocellular enzyme. When the lectin ligand is absent from the algal cell wall, both endocellular and secreted arginases seem to be able to enter algal cells. This uptake promotes the increase in the amount of algal putrescine, preferently as free polyamine, and the chloroplast is rapidly damaged. Induction of cell wall urease retains lectins outside the cells, on the cell wall, and chloroplast remains healthy.
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PMID:Correlationships between enzymatic activity of lectins, putrescine content and chloroplast damage in Xanthoria parietina phycobionts. 774 19

Highly specific detection of human alpha 1-acid glycoprotein (AGP) and asialo-alpha 1-acid glycoprotein (asialo-AGP) was made possible by use of a sandwich immunoassay. The glycoproteins were sandwiched between biotinylated and fluoresceinated polyclonal rabbit anti-human AGP antibodies. Additionally, asialo-AGP could be distinctly detected, apart from AGP, via the formation of a heterosandwich immunoassay using biotinylated polyclonal rabbit anti-human AGP and the lectin, fluoresceinated ricin toxin. Streptavidin was added to the formed immunocomplexes and the immunocomplexes captured on a biotinylated nitrocellulose membrane. The signal generator, urease conjugate of an anti-fluorescein antibody, was then bound to the complex on the membrane. The rate of pH change under microvolume conditions (0.6 microliters) was monitored using a silicon chip-based, light addressable potentiometer sensor. Results indicated that AGP and asialo-AGP can be detected to the 2 pg level when two antibodies are used to form the immunocomplex. Asialo-AGP can be detected down to 250 pg when the heterosandwich immunoassay is used; this assay exhibited no response up to 10 ng for native AGP or asialofetuin. Both immunoassays can be used to quantify the level of AGP and asialo-AGP in solution. Although the assay presented is very specific for AGP, asialo-AGP and terminal galactose, it is readily adaptable for the detection of any glycoprotein and terminal carbohydrate (or branched structure) by use of a protein-specific antibody and various lectins.
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PMID:Detection of human asialo-alpha(1)-acid glycoprotein using a heterosandwich immunoassay in conjunction with the light addressable potentiometric sensor. 887 21

A secreted, glycosylated arginase (lectin) from Xanthoria parietina thallus binds to the cell wall of Xanthoria photobiont when cell wall urease has previously been induced. The uptake of this secreted arginase by the algal cell without cell wall ligand for the lectin increases the concentration of algal putrescine and it is followed by an apparent loss of chlorophyll. However, neither chlorophyllase activity has been detected nor chlorophyllide concentration increases after loading the cells with putrescine. The loss of chlorophyll can be explained by the loss of algal protoplast resulting from the action of a putrescine-activated glucanase and the split of their membrane in an hypoosmotic medium. The loss and split of protoplasts have been shown by light and transmission electron microscopy.
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PMID:Secreted, glycosylated arginase from Xanthoria parietina thallus induces loss of cytoplasmic material from Xanthoria photobionts. 992 41

The research was conducted with two different recently released Brazilian soybean cultivars (Rio Balsas and Bays) to evaluate whether there is any correlation between the different levels of antinutritional and/or toxic proteins in the cultivars and their nutritive value as sources of protein for monogastric animals (rats). Furthermore, it is discussed, for the first time, the role of the dietary soyatoxin on the performance of rats fed on diets containing soyatoxin-rich (cv. Bays) and soyatoxin-free (cv. Rio Balsas) soybean cultivars. Feeding rats with diets containing raw soybean cultivars showed a lower growth rate, net protein utilization and digestibility, a much higher dry matter and nitrogen excretion and macroscopic alterations in internal organs when compared to rats fed on egg-white protein. The nutritional parameters measured for the diet based on raw Bays cultivar were poorer than those of the diet prepared with Rio Balsas. In the raw soybeans, trypsin inhibitor and lectin, and urease to a lesser extent, significantly affected at different fashion the soybean protein utilization. Heating treatment of the Bays seeds increased the growth rate, NPU, in vivo protein digestibility and practically eliminated or attenuated all the organ alterations observed. This study might be helpful in the choice of safe and nutritious soybean cultivars.
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PMID:Nutritional study of two Brazilian soybean (Glycine max) cultivars differing in the contents of antinutritional and toxic proteins. 1117 62

Native soybean lectins (SBL) could potentially have deleterious effects on young animals. The objectives of this study were to determine the optimum processing temperature and time at which SBL is inactivated and to investigate the possibility of using urease activity (UA) to predict residual lectin levels in soybean meal (SBM). Raw defatted SBM was steam-heated at incremental temperatures between 90 and 120 degrees C for 5 to 20 min in an autoclave. The processed meals were subjected to native-PAGE and measurement of total carbohydrate-binding lectin (TCBL), agglutinating lectin (AL), UA, and trypsin inhibitor (TI). Processing severity was evaluated by determining protein solubility in 0.2% potassium hydroxide. Results indicated that levels of all antinutrients (TCBL, AL, UA, and TI) decreased with increasing processing temperature (P < 0.05). The intensity of the lectin band on the electrophoresis gel was considerably reduced when meal was heated at 100 degrees C for 5 min. This result implied that lectin inactivation occurred at 100 degrees C. More than 90% of all the original antinutrient levels in the raw meal were destroyed when meals were heated at 100 degrees C for 5 min. Meals processed at 100 degrees C for 5 to 20 min had protein solubility values (80 to 85%) indicative of adequate processing. The denaturation pattern of UA was highly correlated with that of SBL (r > or = 0.73), indicating that UA could be used for monitoring lectin levels in commercial meals. We concluded that UA of 0.03 to 0.09 units of pH change are indicative of adequately processed meals that contain negligible lectin levels.
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PMID:Investigating the possibility of monitoring lectin levels in commercial soybean meals intended for poultry feeding using steam-heated soybean meal as a model. 1271 Apr 87

Purified arginases secreted from Evernia prunastri and Xanthoria parietina thalli hydrolyze arginine in a Mn2+ -dependent reaction. Ca2+ cannot replace Mn2+, but its addition to reaction mixtures in the presence of Mn2+ significantly inhibited arginase activity. Arginases from both lichen species also show lectin function, binding to the cell wall of both homologous and heterologous algae. Such binding is enhanced by both Ca2+ and Mn2+ and results in cytoagglutination, which is counteracted by alpha-D-galactose. A putative ligand for these lectins consists of a glycosylated urease, the polysaccharide moiety of which is uniquely composed of alpha-D-galactose. Binding of lectins inhibits its enzymatic activity, which is recovered after desorption of the lectin with alpha-D-galactose. Urease is also eluted from arginase-agarose columns by using alpha-D-galactose as eluent. Data demonstrate ligand-dependent retention of the fungal lectin on the algal cell surface and this is consistent with a model of recognition of compatible algae, through which algal cells would form a lichen with a lectin-secreting fungus only when these cells contain the specific ligand for the lectin in their cell walls. This is, lectin binding is used as a mechanism for ensuring specificity in the association.
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PMID:Secreted arginases from phylogenetically farrelated lichen species act as cross-recognition factors for two different algal cells. 1550 67

Concanavalin A, the lectin from Canavalia ensiformis, develops arginase activity depending on Mn(2+). The cation cannot be substituted by Ca(2+) which, in addition, inhibits Mn(2+)-supported activity. Fluorescein-labeled Concanavalin A is able to bind to the cell wall of algal cells recently isolated from Evernia prunastri and Xanthoria parietina thalli. This binding involves a ligand, probably a glycoprotein containing mannose, which can be isolated by affinity chromatography. Analysis by SDS-PAGE reveals that the ligand is a dimeric protein composed by two monomers of 54 and 48 kDa. This ligand shows to be different from the receptor for natural lichen lectins, previously identified as a polygalactosylated urease.
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PMID:Concanavalin A binds to a mannose-containing ligand in the cell wall of some lichen phycobionts. 1559 96

Electropolymerized m-phenylenediamine was used as an active coating for immobilizing urease and lectin on a gold-plated thickness-shear-mode (TSM) crystal. To enhance effectiveness of immobilization. a bilayer polymer film composed of polyaniline and poly-m-phenylenediamine was proposed. Compared with single poly-m-phenylenediamine film, the bilayer polymer film gave better results in terms of immobilizing capacity, stability and reproductivity. On this bilayer-film-coated TSM quartz crystal, the amount of immobilized lectin was estimated about 1.8 mug/cm(2). Detection of purified human erythrocytes is demonstrated as an example of potential application of this lectin-modified TSM biosensor in clinic.
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PMID:Electropolymerized m-phenylenediamine as a means to immobilize active protein on thickness-shear-mode quartz crystal. 1896 54


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