Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.31 (beta-glucuronidase)
7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Defensins are a newly recognized class of small, cationic polypeptides that have in vitro microbicidal activity toward certain bacteria, fungi, and viruses. Human neutrophil granules were separated into 13 density fractions by using a high-resolution Percoll gradient centrifugation procedure, and the distribution of the three defensin polypeptides in these fractions was determined. Levels of defensins and several granule marker proteins were estimated in each fraction from relative staining intensities of bands following acid-urea and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of total acid-extractable proteins. These results were confirmed by enzyme immunoassay measurements of defensins and quantitative determinations of the typical azurophil granule components, myeloperoxidase, beta-glucuronidase, lysozyme, and elastase. The five higher density granule fractions (H1 through H5) contained fourfold higher relative amounts of defensins as compared with the eight lower density fractions (L1 through L8), accounting for approximately 50% of the total protein. In particular, fraction H5 was especially enriched in defensins but was relatively deficient in myeloperoxidase, beta-glucuronidase, lysozyme, and elastase. Ultrastructural morphology showed that fraction H5 contained the largest granules. Seventy percent of these granules exhibited electron-dense rims and electron-lucent central regions when stained with methanolic uranyl acetate-lead citrate, and 70% showed this same characteristic rim-staining pattern after limited reaction (30 minutes) for peroxidase with diaminobenzidine. These distinctively large, rim-stained granules were identified in intact, mature peripheral blood neutrophils as well as in human bone marrow promyelocytes, indicating that their synthesis occurs during early myeloid development. This unusual granule type may play a specialized role in the microbicidal functions of the neutrophil, distinct from that of typical azurophil granules.
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PMID:Defensin-rich dense granules of human neutrophils. 304 Jan 55

Homogenates of Giardia lamblia trophozoites exhibited the following hydrolase activities: acid phosphatase (EC 3.1.3.2), proteinase (EC 3.1.4) with urea-denatured hemoglobin and N-benzoyl-DL-arginine-2-naphthylamide as substrates, deoxyribonuclease (EC 3.1.4.5), and ribonuclease (EC 2.7.7.16). beta-N-Acetylglucosaminidase (EC 3.2.1.30), beta-galactosidase (EC 3.2.1.23), beta-glucuronidase (EC 3.2.1.31), alpha-D-glucosidase (EC 3.2.1.20), beta-D-glucosidase (EC 3.2.1.21), and beta-D-xylosidase (EC 3.2.1.37) activities were below the level of detection. Differential and isopycnic centrifugation of homogenates demonstrated that giardial hydrolases were localized in a single-particle population sedimenting at 7200g for 30 min. The particles had a buoyant density in sucrose of 1.15 and exhibited latency. Latency was completely destroyed by Triton X-100 or 15 cycles of freezing and thawing. After centrifugation of Triton- or freeze-thaw-treated particle fractions, the hydrolase activities, though no longer latent, were still sedimentable suggesting tight binding to the organelle membrane. Latency was destroyed simultaneously for all hydrolases, in direct proportion to the amount of Triton added to a particle preparation or to the number of times a particle preparation was subjected to freezing and thawing. These results support the suggestion that the hydrolases of G. lamblia trophozoites are localized in a single-particle population of lysosome-like organelles.
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PMID:Giardia lamblia: localization of hydrolase activities in lysosome-like organelles of trophozoites. 327 50

In our laboratory, selected strains of Gram-negative rods from urine samples are identified as Escherichia coli on the basis of smell and morphology on lactose agar. To investigate the accuracy of this routine practice, 211 consecutive strains were tested in the urea-indole tube of the Three-tube method (3-TM), in the PGUA test detecting beta-glucuronidase activity and in the Simmons' citrate test, to select the strains that were non-E. coli. Additional 1022 strains were tested by the indole and urease tests of the 3-TM only. The identification of E. coli based on the macroscopic evaluation of colonies on lactose agar gave correct results for 99.1% of the strains. Citrobacter freundii was the most frequent cause of erroneous identification.
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PMID:Rapid identification of Escherichia coli from routine urine specimens based on macroscopic criteria. 391 21

1. beta-Glucuronidase (EC 3.2.1.31) was purified from rabbit liver by a procedure involving autolysis, (NH(4))(2)SO(4) fractionation, chromatography on DEAE-cellulose and hydroxyapatite, gel filtration, sedimentation in a sucrose gradient, and isoelectric focusing. 2. Electron microscopy revealed ferritin as the major contaminant in later stages of purification and also showed aggregates of enzyme molecules. Particular attention was paid to the removal of ferritin. 3. The purified enzyme was homogeneous in polyacrylamide-gel electrophoresis both in non-dissociating conditions and in the presence of sodium dodecyl sulphate, and in Ouchterlony gel diffusion and immunoelectrophoresis against polyspecific antisera. 4. Sedimentation in sucrose gradients gave a molecular weight of 300000, whereas gel filtration indicated 440000. 5. Subunits of 75000 molecular weight were observed in gel electrophoresis in the presence of sodium dodecyl sulphate and in gel filtration in the presence of urea. 6. The K(m) value for p-nitrophenyl beta-d-glucuronide was 0.6mm, and the enzyme was extremely sensitive to lactone inhibitors. It was also inhibited by Hg(2+) ions. 7. Multiple forms were observed in the pure enzyme by isoelectric focusing, with pI values of 4.5-5.8. Subunits showed similar heterogeneity. The origin of the multiple forms was investigated in detail, and the possibility of artifact generation largely excluded. Some of the forms of lowest pI disappeared after neuraminidase digestion. The nature of the residual heterogeneity remains to be elucidated.
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PMID:Rabbit beta-glucuronidase. Purification and properties, and the existence of multiple forms. 421 18

The beta-glucuronidase activity of Drosophila melanogaster exists as two chromatographically separable forms, both of which are glycoproteins. Form I is membrane-bound in vivo, has a pI of 8.0-8.5, and can be irreversibly inactivated either by incubation at 55 degrees C for 20 min or by incubation at 37 degrees C in the presence of 6 M urea. Form II exists both membrane-bound as well as membrane-free, has a pI of 4.5, and is resistant to the conditions which inactivate form I. The two forms are similar in Km and Vmax for the artificial substrate 4-methylumbelliferyl-beta-D-glucuronide and both forms are precipitated by antibody to form II. A natural genetic variant, beta-GluL1, completely lacks from I beta-glucuronidase. This variant behaves in a co-dominant fashion for the determination of the presence of form I and has been localized to the extreme distal portion of chromosome 3R. Other data indicate that at least one genetic determinant for the amount of form II is also localized to this portion of chromosome 3R.
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PMID:A genetic variant of beta-glucuronidase in Drosophila melanogaster. 640 73

Myxococcus coralloides D was found to produce a substance with a narrow range of antibacterial activity. This substance was produced during the exponential growth phase and was not inducible by ultraviolet light or mitomycin C treatment. The bacteriocin was precipitable by ammonium sulphate, and showed resistance to heat (100 degrees C for 10 min), trypsin, lysozyme, beta-glucuronidase, DNase, RNase, acetone, ethyl ether, urea and mercaptoethanol; it was partially destroyed by pronase and inactivated at extreme pH values. Electron microscopy did not reveal any phage-like particles associated with bacteriocin activity.
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PMID:Production and properties of a bacteriocin from Myxococcus coralloides D. 643 23

Biochemical analysis of 328 human prostatic fluid samples were performed. The urea concentration of 69 samples was similar to that of serum and not indicative of significant contamination with urine. The pH of normal fluids was acidic (mean pH = 6.7). The interrelationships between zinc, citrate, acid phosphatase aminopeptidase, beta-glucuronidase, diamine oxidase and pH were investigated by factor analysis. Two significant factors were extracted, the first accounted for 89% of their common variance and the second for 11%. Zinc, citrate, acid phosphatase and aminopeptidase were positively and pH was negatively related to factor one. Beta-glucuronidase was positively related to factor two and diamine oxidase was largely independent of both factors. It was concluded that variables related to factor one share a common secretory control and mechanism, that some other mechanism operates in the case of beta-glucuronidase and that diamine oxidase may not be a true secretory product of the prostate.
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PMID:The interrelationships between acid phosphatase, aminopeptidase, diamine oxidase, citric acid, beta-glucuronidase, pH and zinc in human prostatic fluid. 681 44

A nephropathy with severe tubular atrophy was observed in Beagle dogs after oral administration of K2HPO4 for 14 or 38 weeks. We describe the complete lysosomal degradation of atrophying tubular epithelial cells. During two experiments of 14 and 38 weeks duration, respectively, a total of 15 Beagle dogs received 0.8 g K2HPO4/kg body weight daily with their food. All dogs were examined clinically at regular intervals. Renal biopsies were taken in the fourth week from beagles of the 14-week study. Results were compared with those of control dogs. At the end of the experiments the animals were killed and necropsies done. Different stains and histochemical reactions were applied to paraffin sections of the kidneys. Acid phosphatase and beta-glucuronidase were found on cryostat sections. Kidneys fixed by perfusion of five Beagles from the 38-week study and three Beagles of the 14-week study, and from five control dogs, were examined electron microscopically. Ultrahistochemically, acid phosphatase was demonstrated. Clinically, the dogs in both experiments vomited, were cachectic, and had elevated creatinine and blood urea nitrogen. Morphologically, qualitatively identical changes were seen, but the renal damage was most marked at 38 weeks. There were disseminated tubular atrophy (usually of the proximal tubules), focal scar tissue and nephrocalcinosis. The following pathogenesis was established for the lesions of the proximal tubule: Tubular atrophy begins with loss of differentiation of epithelial cells. Enzyme histochemistry, ultrahistochemistry and electron microscopy show an increase in autophagic vacuoles and autophagolysosomes. The lysosomal bodies showing fusion enclose large parts of the cytoplasm as the process continues. Complete lysosomal degradation of epithelial cells and extrusion of large lysosomes into the tubular lumen follow. After complete enzymatic digestion of the intratubular detritus, the residue is empty, convoluted and collapsed tubular basement membrane. Atrophic tubular epithelial cells have many organelle-free zones at their base, which contain fine filamentous material resembling that of the basement membrane. The degradation process described here may explain why clinically the urinary sediment contains few cylinders and epithelial cells and why proteinuria decreases significantly toward the end of the experiment. So far, it is not clear whether the tubular basement membrane is synthesized by the tubular cells, by fibroblasts or by both cell types. The presence of basement membrane-like material in tubular epithelial cells and in parietal epithelial cells of the glomerulus favors the view that epithelial cells produce the basement membranes and that increased production of basement membrane-like material is a sign of loss of differentiation.
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PMID:[Potassium hydrogen phosphate induced nephropathy in the dog. I. Pathogenesis of tubular atrophy (author's transl)]. 742 30

We studied 12 coryneform isolates having similar biochemical profiles which did not permit their assignment to any recognized taxa. Human semen was the source for seven of these strains, whereas the other strains were isolated from urethra, urine, and blood specimens of adult male patients. These bacteria were found in significant quantities (10(4) to 10(5) CFU/ml) in semen specimens from infertile male patients with the diagnosis of prostatitis. These strains had characteristics of the genus Corynebacterium, such as 60 mol% G + C in the DNA and corynemycolic acids, meso-diaminopimelic acid, arabinose, and galactose in the cell wall. Quantitative DNA-DNA hybridizations (S1 nuclease procedure) and phylogenies based on comparisons of almost-complete small-subunit ribosomal DNA sequences confirmed that these strains constitute a single new species within the genus Corynebacterium. All 12 strains showed similar phenotypic features, i.e., good growth on sheep blood agar in contrast with poor growth on the same medium supplemented with 1% Tween 80, a positive CAMP test in the presence of Staphylococcus aureus, glucose and sucrose fermentation, and the presence of beta-glucuronidase. Some strains reduced nitrate and hydrolyzed urea or esculin. These features allowed us to distinguish these strains from members of any other coryneform taxon, and the proposed name is Corynebacterium seminale with strain IBS B12915 (CIP 104297) as the type strain. The description and delineation of these strains as a new species should be useful for further studies, including evaluations of their prevalence among the normal flora and their clinical implications.
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PMID:Corynebacterium seminale sp. nov., a new species associated with genital infections in male patients. 749 9

Factor J (FJ) is a new inhibitor of the complement system. This work supports the fact that FJ is a cationic molecule (pI > or = 9.6 in native conditions, or pI = 8.1 in denaturing conditions) with a high sugar content (40%) that is able to interact with different lectins, suggesting a complex glycosylation. SDS impaired FJ migration in polyacrylamide gel electrophoresis. In Triton-acid-urea-polyacrylamide gel electrophoresis FJ migrated as a complex, dispersed molecule. In contrast, FJ after Smith degradation (dFJ) gave a single, smeared band of M(r) = 23.4 kDa in reducing SDS-PAGE. dFJ retained only 60% of the initial inhibitory activity of intact FJ. When digestions with different proteinases were performed, no modification of activity was observed. After beta-glucuronidase digestion, FJ lost 80% of its initial activity. Consequently, glycosylation plays an important role in the inhibitory activity of FJ.
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PMID:Factor J, a human inhibitor of complement C1, is a cationic, highly glycosylated protein. 789 Mar 18


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