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:3.2.1.31 (beta-glucuronidase)
7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The dodecasaccharide obtained by treating dermatan sulfate with testicular hyaluronidase, chondroitinase AC, and beta-glucuronidase was incubated with diluted, normal human serum at pH 4.5 or 7.0 followed by chondro-4-sulfatase at pH 7.0. Analyses of the reaction products indicate release of hexosamine but not further degradation of the substrate. It is concluded that normal human serum possesses an exo-beta-N-acetylhexosaminidase active on dermatan sulfate.
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PMID:Beta-N-acetylhexosaminidase active on dermatan sulfate. 109 49

In order to obtain sufficient quantities of beta-glucuronidase for use in structural studies, the enzyme was purified from its richest known source, the female rat preputial gland, by a method similar to that of Ohtsuka and Wakabayashi (1969) (Enzymologia 12, 109). The purified enzyme has an S-o20, w of 12.5 S and a D-o20, w of 4.3 times 10- minus 7 cm-2 S-minus 1. Sedimentation diffusion and sedimentation equilibrium yielded molecular weights of 267,000 and 283,000, respectively. The limiting viscosity (3.6 ml/g) and the f/fo (1.08 at sigma equals to 0.2 g of H2O/g of protein) indicate that the enzyme is a typical globular protein possessing little asymmetry. The circular dichroism spectrum indicates approximately 14% alpha-helix and a far greater amount of random coli than beta structure. The enzyme is acidic, having an isoelectric point of 6.15. In electrophoresis on polyacrylamide gels containing sodium dodecyl sulfate the enzyme exhibits a single band at molecular weight 72,000, a result indicating that the enzyme consists of four subunits of similar molecular weight. Tryptic peptide mapping suggests that the subunits are identical.
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PMID:Physical and chemical properties of beta-glucuronidase from the preputial gland of the female rat. 114 Dec 28

The turnover of rat liver lysosomal proteins was studied by a double isotope-labeling technique. The cellular fractions investigated included soluble lysosomal proteins, lysosomal membrane proteins, highly purified lysosomal beta-glucuronidase, and for comparison, microsomal proteins and soluble cytoplasmic proteins. Both "normal" lysosomes and Triton WR-1339-filled lysosomes (tritosomes) were studied, with similar results. It was found that (a) the turnover rate of lysosomal proteins, of both the soluble and membranous compartments, was very similar to that of the proteins of the microsomal and soluble cytoplasmic fractions, and (b) the turnover rate of lysosomal proteins was asynchronous. The latter conclusion was based on two lines of evidence: (a) lysosomal beta-glucuronidase had a distinctly slower turnover rate than the average rate of the soluble lysosomal proteins, and (b) subunits of the proteins of the soluble lysosomal fraction as separated by sodium dodecyl sulfate. Sephadex G-200 gel filtration showed different rates of degradation.
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PMID:Turnover studies on proteins of rat liver lysosomes. 115 Jun 46

The metabolism and excretion of silybin (as N-methyl-glucamine salt) was investigated after intravenous and oral administration to rats. In the urine, silybin was excreted mostly in the unchanged form after intravenous as well as oral application, whilst in the bile it appeared above all in the form of metabolites. By hydrolysis with arylsulfatase/beta-glucuronidase, the metabolites were identified as sulfate and glucuronide conjugates of silybin and dehyrosilybin; the latter appeared in small quantities as a dehydrated product of silybin. After intravenous injection of 20 mg silybin per kg body weight, the excreted amount of silybin after 48 h was 8%, whereas 76% was eliminated in the bile within the same period of time. After oral application of 2--20 mg silybin/kg body weight 20% after 40 mg/kg 35% and after 120 mg/kg 20% of the administered silybin was excreted in the bile during 48 h. The maximum excretion rate was achieved at application of 20 mg/kg p.o. after 1 h. At this dosage, 2--5% was eliminated within the same time in the urine. The excretion of silybin mainly took place (more than 80% of the total of excreted bilybin) in the bile, both after oral and intravenous administration.
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PMID:[Studies of the metabolism and excretion of silybin in the rat]. 117 27

The lysosomal form (L form) of beta-glucuronidase was purified 6,500-fold from the liver of C57BL/6J mice with high yield. Purified enzyme was homogeneous as judged by polyacrylamide gel electrophoresis in the presence or absence of sodium dodetcyl sulfate. The microsomal forms of beta-glucuronidase were spontaneously converted to the L form. The purified L form is a tetramer of molecular weight of 280,000 to 300,000, composedd of four identical subunits of 75,000 molecular weight. The enzyme contains a high content of arginine and glutamic acid and a very low content of sulfur-containing amino acids. Approximately 7% of the enzyme molecule is compose of carbohydrate. Sugars in the L form are glucosamine, mannose, galactose, and glucose. Sialic acid and fucose are absent in the enzyme.
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PMID:Purification and chemical properities of mouse liver lysosomal (L form) beta-glucuronidase. 119 64

Immune arthritis in sensitized rabbits was induced by intraarticular injection of bovine serum albumin. The development of the arthritis was accompanied by an increase in ESR, a rise of the level of serum CRP, caeruloplasmin and CIC. A chemiluminescent response of the whole blood phagocytes to stimulation by barium sulfate crystals, serum beta-glucuronidase and red cell superoxide dismutase activity enhanced, plasma malone dialdehyde content rose, serum SH groups diminished.
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PMID:[The effect of intra-articular emoxipin injections on the course of immune arthritis in rabbits]. 128

Urine samples containing diazolo- and triazolobenzodiazepines and metabolites were hydrolyzed with beta-glucuronidase and extracted with methylene chloride. The extracts were treated with methyl iodide, methylene chloride, and tetrahexylammonium hydrogen sulfate in basic solution to form the methyl derivatives of the drugs and metabolites. GC/MS analysis resulted in the following test characteristics: day-to-day precision at 360 ng/mL (120 ng/mL for the triazolobenzodiazepine metabolites) was 2.4 to 5.5% CV; calibration curves were linear to 6000 ng/mL (1000 ng/mL for the triazolobenzodiazepine metabolites), and operational limits of quantitation were in the range 13-25 ng/mL.
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PMID:Confirmation of low concentrations of urinary benzodiazepines, including alprazolam and triazolam, by GC/MS: an extractive alkylation procedure. 129 2

beta-Glucuronidase from bovine liver was adsorbed to the adsorbents prepared with CH-Sepharose 4B and either the competitive inhibitor or its analogs such as p-aminophenyl 1-thio-beta-D-glucuronic acid, -glucoside, -galactoside, and N-acetyl glucosaminide. The adsorbed enzyme was eluted at 0.1 or 0.5 M NaCl by a stepwise gradient. Chromatography of the enzyme was also performed by using the adsorbents prepared with Epoxy-activated Sepharose 6B and amine compounds or other compounds. In order to see whether the hydroxyl groups of the sugar parts in the ligand are necessary for the adsorption of the enzyme, chromatography was performed by using the adsorbents prepared with sugar derivatives as the ligand. As a result, it was found that beta-glucuronidase had an affinity for adsorbents prepared with either acetyl derivatives or methoxy derivatives of glycosides and CH-Sepharose 4B. From the results of elution of the enzyme with NaCl from adsorbents having amide bonding, it was clarified that the affinity of the enzyme for adsorbents without glycosides in the ligands correlated with acidity of the amide in the adsorbents. Hydrogen bond chromatography was performed with the prepared adsorbents. The enzyme was adsorbed under a high concentration of ammonium sulfate, and the elution of the adsorbed enzyme from adsorbents was examined by the degradation of salt. The enzyme was most easily eluted from aminoethyl 1-thio-beta-D-glucuronic acid-CH Sepharose 4B at 0.9 M ammonium sulfate and at 0.5 M concentration of the salt with p-aminophenyl 1-thio-beta-D-glucuronic acid-CH Sepharose 4B.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Chromatography of beta-glucuronidase from bovine liver. A study of the enzyme binding sites of prepared adsorbents. 139 4

The antiprotozoal drug pentamidine [1,5-bis(4'-amidinophenoxy)pentane] has been previously shown to be metabolized by rat liver microsomes, and five of the seven putative primary metabolites have been identified. With the synthesis and identification of 5-(4'-amidinophenoxy)pentanoic acid and 5-(4'-amidinophenoxy)-1-pentanol as the remaining two metabolites, the primary metabolism of pentamidine in rats appears fully characterized. Use of [14C]pentamidine with rat liver microsomes confirms this conclusion, since no unidentified radioactive peaks were detected by high-performance liquid chromatography (HPLC). Isolated, perfused rat livers were used with [14C]pentamidine to identify secondary metabolites. Only two novel radioactive peaks were detected by HPLC analysis of perfused liver samples. The treatment of liver samples with sulfatase or beta-glucuronidase resulted in the reduction or elimination of these peaks and gave rise to peaks identified as para-hydroxybenzamidine and 5-(4'-amidinophenoxy)pentanoic acid. It was concluded from these results that only these two primary metabolites were conjugated with sulfate or glucuronic acid. After 4 h of incubation in the perfused liver system, approximately 15% of the recovered radiolabel was pentamidine. These results suggest that pentamidine metabolism can be rapid and extensive in rats.
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PMID:Primary and secondary metabolism of pentamidine by rats. 141 74

[3H]Benzo[a]pyrene (B[a]P) was administered to male Sprague-Dawley rats via intratracheal instillation, and bile was collected over a period of 6 h. Conjugated metabolites of B[a]P in bile were separated by paper chromatography or reversed-phase ion-pair HPLC and quantified by liquid scintillation spectrometry. In paper chromatographic analysis, a class of conjugates more polar than thioether conjugates was recognized. These conjugates were identified as quinol diglucuronides by hydrolyzing with beta-glucuronidase and analyzing products of the hydrolysis with HPLC, and by migration on paper relative to a standard of 3,6-quinol diglucuronide. From this analysis, relative amounts of conjugated metabolites of B[a]P in bile were 37.3% quinol diglucuronides, 19.9% thioether conjugates, 33.3% monoglucuronide and sulfate conjugates, and 9.4% unconjugated metabolites. Analysis by reversed-phase ion-pair HPLC provided improved resolution among the conjugates in bile. In particular, the 3,6-quinol diglucuronide was resolved from the 1,6- and 6,12-quinol diglucuronides, with identification of peaks being based on sensitivity to hydrolysis with beta-glucuronidase and elution of standards of these diglucuronides. The elution position of thioether conjugates was identified by their insensitivity to hydrolysis with beta-glucuronidase and arylsulfatase and by synthesis of thioether conjugates in V79 (XEM-2) cells, which express cytochrome P450IA1 and have relatively high levels of glutathione S-transferases but low levels of UDP-glucuronyltransferases and sulfotransferases. From the reversed-phase ion-pair HPLC analysis, relative amounts of conjugates in bile were 10.4% 1,6- and 6,12-quinol diglucuronides, 20.8% 3,6-quinol diglucuronide, 30.4% thioether conjugates, 17.8% monoglucuronides, 6.2% sulfate conjugates, and 14.4% unconjugated metabolites. These studies provide the first report of the biosynthesis of quinol diglucuronide conjugates of B[a]P in vivo and demonstrate that they are excreted into bile in significant quantities.
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PMID:Quinol diglucuronides are predominant conjugated metabolites found in bile of rats following intratracheal instillation of benzo[a]pyrene. 154 30


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