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

Actinomyces pyogenes (Corynebacterium pyogenes), a well-known pathogen in many animals, was isolated from 11 Danish patients since 1968. Bacteriologic characteristics and clinical pictures of the patients are described. Ability to hydrolyze gelatine, to produce beta-glucuronidase, to reach with antisera against group-G streptococci, and to produce acid from xylose differentiates A. pyogenes from Arcanobacterium haemolyticum, with which it has at times been confused. Actinomyces pyogenes is an established, but often misrecognized, human pathogen that should be better known to clinical microbiologists.
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PMID:Human infections with Actinomyces pyogenes (Corynebacterium pyogenes). 161 50

Human urinary chondroitin sulfates were isolated by precipitation with cetylpyridinium chloride of the non-dialyzable fraction of pooled urine, followed by ethanol fractionation and successive enzymic digestions with neuraminidase and mucopolysaccharides. Further purification was achieved by Dowex-1 chromatography with stepwise elution by increasing the concentration of NaCl at intervals of 0.25 M from 0.75 M to 1.5 M. The chondroitin sulfates thus obtained were characterized by the analysis and quantification on of carbohydrate, amino acid and sulfate, and by electrophoresis on cellulose acetate membrane. Then reducing terminals were identified by gas liquid chromatographic analyses of the acetyl and butaneboronate derivatives of hydrolysates, after reduction of the reducing terminals with sodium borohydride. About 22.8% of the urinary chondroitin sulfate in the 1.5 M fraction was peptide-bound, and the remainder was peptide-free, with xylose (29.8%), galactose (23.6%) and glucuronic acid (18.7%) at the reducing terminal. The amount of peptide-free chondroitin sulfate with xylose and galactose at its reducing terminals in the 0.75 M-, 1.0 M-, 1.25 M- and 1.5 M-fractions increased in the order described in parallel with the increase of sulfation and the decrease of peptide content. It was thus suggested that the endo-types of beta-xylosidase, beta-galactosidase and beta-glucuronidase acted on the carbohydrate-peptide linkage region of proteo-chondroitin sulfate in the tissues and produced various types of urinary chondroitin sulfate with heterogeneity at reducing terminals.
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PMID:Heterogeneity of reducing terminals of urinary chondroitin sulfates. 310 93

Human urinary chondroitin sulfate isolated from the cetylpyridinium chloride-complex of the non-dialyzable fraction of the pooled urine was subjected to ethanol fractionation, successive enzymic digestion with neuraminidase and mucopolysaccharidases, and anion exchange chromatography. The gas liquid chromatographic analyses of the acetyl and butaneboronic acid ester derivatives of the reduced terminal sugar units after treatment with sodium borohydride plus hydrolysis revealed that 42% of the urinary chondroitin sulfate was bound to peptide through xylose. The reducing terminal sugar units of the peptide-free form consisted of 34.6% of xylose, 22.4% of galactose, 16.4% of glucose of unknown origin and 26.6% of glucuronic acid. These observations showed that the xyloside, galactoside and glucuronide linkages at non-terminal sites of carbohydrate chains of chondroitin sulfate were cleaved in tissues. It was thus suggested that the endo-types of beta-xylosidase, beta-galactosidase and beta-glucuronidase, which act on proteochondroitin sulfate are present in tissues.
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PMID:Reducing terminals of urinary chondroitin sulfate. 393 89

To elucidate the mode of the exertion of glycosidase activities in the catabolism of the tissue glycosaminoglycans (GAG), the terminal monosaccharides of the carbohydrate chains of urinary GAG in the most prominent subfraction (40% Fr-1.25 M Fr) among the subfractions obtained in a previous paper (Endo et al. 1980a) were investigated. The results of determination of the reducing hexuronic acid and N-acetylhexosamine before and after digestion of the subfraction with beta-glucuronidase and beta-N-acetylhexosaminidase, together with previous data indicated that 0.36 and 0.37 mol of glucuronic acid and N-acetylgalactosamine, respectively, per mol of the subfraction were located at the non-reducing terminals of the carbohydrate chains. The remaining portion (0.27 mol per mol) of the non-reducing ends might be mostly occupied by the sulfated N-acetylgalactosamine residues. On the other hand, 0.25, 0.16 and 0.34 mol of glucuronic acid, N-acetylgalactosamine and xylose, respectively, per mol of the subfraction were indicated to the present at the reducing terminals of the carbohydrate chains. The remaining portion (0.25 mol per mol) of the reducing ends might be mostly occupied by the galactose residues and/or the N-acetylgalactosamine 4-sulfate residues. The present observations provided with evidence for the action of endo-beta-glucuronidase and endo-beta-N-acetylhexosaminidase on the tissue GAG, specifically on chondroitin sulfates.
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PMID:Terminal monosaccharides of carbohydrate chains of glycosaminoglycans in normal human urine. 720 66

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

We previously described a diverse family of sulfated anionic N-linked oligosaccharides released by peptide: N-glycosidase F (PNGaseF) from calf pulmonary artery endothelial (CPAE) cells (Roux, L., Holoyda, S., Sundblad, G., Freeze, H.H., and Varki, A. (1988) J. Biol. Chem. 263, 8879-8889). Since a major fraction of the intact lung consists of endothelial cells, we reasoned that bovine lung might be a rich source of similar molecules. Total N-linked oligosaccharides from bovine lung acetone powder were released by PNGaseF, labeled by [3H]NaBH4 reduction, and the anionic fractions were studied with a variety of techniques. The sugar chains with lesser negative charge (designated Class I) share several properties of conventional multiantennary complex-type chains. However, unlike the case with CPAE cells, sialic acids account only for a minority of the anionic properties and only a small proportion carry sulfate esters. A variety of different treatments indicate that most of the unexplained negative charge is due to multiple carboxylic acid groups. Resistance to beta-glucuronidase and alpha-iduronidase suggests that these may be previously undescribed modifications of mammalian oligosaccharides. The most highly charged N-linked chains (designated Class II) are more similar in general structure to the corresponding ones from CPAE cells, although relatively more abundant. Their high charge is primarily due to chondroitin sulfate, heparin/heparan sulfate, or keratan sulfate glycosaminoglycan chains. Sequential digestion studies suggest that a significant proportion of these molecules have more than one type of glycosaminoglycan chain associated with them. Compositional analysis indicates the presence of xylose residues in Class II, but not Class I molecules. However, unlike the case with conventional glycosaminoglycans, these residues are not at the reducing terminus. Most previously reported structures of complex-type N-linked oligosaccharides are derived from the glycoproteins of blood cells, plasma, or the secretions of cultured mammalian cells. This library of N-linked oligosaccharides from an intact mammalian organ (lung) contains a high proportion of novel anionic sugar chains whose structures are different from conventional complex-type sialylated chains and only partially related to those from CPAE cells. Further exploration of the N-linked chains of intact mammalian tissues seems warranted.
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PMID:Unusual anionic N-linked oligosaccharides from bovine lung. 749 28

The regulation of transcription of the glucoamylase-encoding gene (glaA) of Aspergillus niger was studied. To facilitate this study a reporter strain containing a fusion of the glaA promoter (PglaA) of A. niger to the beta-glucuronidase-encoding gene (uidA) of Escherichia coli was constructed. To analyze whether regulatory proteins are involved in the regulation of glaA, multiple copies of PglaA were introduced into this reporter strain. Analysis of the resulting strains revealed that introduction of an increasing number of PglaA copies resulted in lower expression of the uidA reporter gene and the endogenous glaA gene in cultures cultivated on different inducing carbon sources. However, repression by xylose was not influenced by the copy number of PglaA. These results indicate that the expression of genes under control of PglaA are regulated by specific trans-acting regulatory protein(s). Deletion analysis of PglaA indicated that regulatory proteins interact with DNA sequences within 0.5-kb upstream from the ATG, whereas sequences between about 0.8- and 0.5-kb upstream from the ATG are required for high-level expression of glaA.
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PMID:The effect of multiple copies of the upstream region on expression of the Aspergillus niger glucoamylase-encoding gene. 805 29

A novel culture medium for cultivation of fastidious oral anaerobes is described. This medium, OMIZ-Pat, consists of a rich chemically defined basal medium supplemented with asialofetuin, as well as yeast extract and Neopeptone fractions. Addition of 1 mg of rifampin per liter and 100 mg of fosfomycin per liter allowed routine isolation of spirochetes by a limit dilution method in 96-well plates containing liquid OMIZ-Pat. In addition to members of the four previously recognized species of oral treponemes (Treponema denticola, Treponema pectinovorum, Treponema socranskii, and Treponema vincentii), 26 previously undescribed spirochete strains belonging to one group were isolated. We propose the name Treponema maltophilum sp. nov. for these small spirochetes, which have two endoflagella; one endoflagellum is attached at each cell pole, and the endoflagella overlap in the middle of the cell. Growth of these organisms was dependent on a carbohydrate like D-arabinose, L-fucose, D-maltose, L-rhamnose, D-ribose, D-sucrose, or D-trehalose and was inhibited by fetal bovine serum. T. Maltophilum is distinguished from other oral Treponema species by its 16S rRNA sequence, its protein and antigen patterns as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting, and its characteristic alpha-glucosidase activity. The strains included in the new species on the basis of their 16S rRNA sequences are heterogeneous with respect to their alpha-fucosidase, and beta-glucuronidase activities, their dependence on N-acetylglucosamine, and their antigens as detected with patient antibodies. Strain BR is designated the type strain, and strains HO2A and PNA1 are reference strains of the new species.
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PMID:Treponema maltophilum sp. nov., a small oral spirochete isolated from human periodontal lesions. 878 84

In this study, induction and repression kinetics of the expression of the Aspergillus awamori 1,4-beta-endoxylanase A (exlA) gene under defined physiological conditions was analyzed at the mRNA and the protein levels. Induction was analyzed by pulsing D-xylose to a sucrose-limited continuous culture of an A. awamori 1,4-beta-endoxylanase A (EXLA)-overproducing strain. Directly after the D-xylose pulse, exIA mRNA was synthesized, and it reached a constant maximal level after 45 to 60 min. This level was maintained as long as D-xylose was present. The kinetics of mRNA synthesis of the genes encoding Thermomyces lanuginosa lipase (lplA) and Escherichia coli beta-glucuronidase (uidA), which were also under the control of the exlA promoter, were similar to those observed for exlA mRNA. The repression of exlA expression was analyzed by pulsing D-glucose to a D-xylose-limited continuous culture. Immediately after the glucose pulse, the exlA mRNA level declined rapidly, with a half-life of approximately 20 to 30 min, and it reached a minimal level after 60 to 90 min. The time span between mRNA synthesis and the secretion of proteins was determined for EXLA and lipase. In both cases, mRNA became visible after approximately 7.5 min. After 1 h, both proteins became detectable in the medium but the rate of secretion of EXLA was faster than that of lipase.
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PMID:Kinetics of mRNA and protein synthesis of genes controlled by the 1,4-beta-endoxylanase A promoter in controlled fermentations of Aspergillus awamori. 883 19

A new, highly inducible fungal promoter derived from the Aspergillus awamori 1,4-beta-endoxylanase A (exlA) gene is described. Induction analysis, carried out with the wild-type strain in shake flasks, showed that exlA expression in regulated at the transcriptional level. Using a beta-glucuronidase (uidA) reporter strategy, D-xylose was shown to be an efficient inducer of the exlA promoter, whereas sucrose or maltodextrin were not. Upon D-xylose induction, the exlA promoter was threefold more efficient than the frequently used A. niger glucoamylase (glaA) promoter under maltodextrin induction. Detailed induction analyses demonstrated that induction was dependent on the presence of D-xylose in the medium. Carbon-source-limited chemostat cultures with the uidA reporter strain showed that D-xylose was also a very good inducer in a fermenter, even in the presence of sucrose.
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PMID:An expression system based on the promoter region of the Aspergillus awamori 1,4-beta-endoxylanase A gene. 898 32


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