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

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.
...
PMID:Heterogeneity of reducing terminals of urinary chondroitin sulfates. 310 93

Evidence indicates that lysosomal enzymes can carry out corneal autolysis during corneal storage and that they are damaging to the corneal endothelium. The authors investigated the release of lysosomal enzymes into two corneal storage media (K-Sol and McCarey-Kaufman [M-K]) by paired human donor corneas during 4 degrees C storage. The authors also studied the interaction of these media with lysosomal enzymes from human cornea. K-Sol and M-K stimulated (P less than 0.01) both beta-glucuronidase and alpha-galactosidase about equally. beta-N-Acetyl-glucosaminidase, a major catabolic enzyme of the cornea, was inhibited by the chondroitin sulfate in K-Sol by over 90% (P less than 0.01). Corneas stored in M-K released more lysosomal enzymes than corneas stored in K-Sol. At 4 days, the values approached significance (P less than 0.06) and by day 10 significantly higher values were found in the M-K media (P less than 0.01). Both storage methods showed a linear release. Individual corneas were found to vary in their release rates. Whether corneas that release more enzyme will show higher endothelial cell loss or produce less successful penetrating keratoplasty grafts deserves further study.
...
PMID:Lysosomal enzyme levels in corneal storage media. K-Sol versus McCarey-Kaufman. 314 77

We studied two cases of beta-glucuronidase deficiency. One patient's disease was present at birth and the other patient's disease appeared in early childhood. The symptoms observed in both patients, although of differing severity, included peculiar facies, cloudy cornea, hepatosplenomegaly, hernia, kyphosis, recurrent infections, short stature, and developmental delay, as well as increased excretion of urinary chondroitin sulfate A/C and decreased levels of beta-glucuronidase activity. We reviewed all of the reported cases and examined the biochemical and clinical heterogeneity observed in this disorder.
...
PMID:Beta-glucuronidase deficiency. A heterogeneous mucopolysaccharidosis. 315 9

Eighteen patients with total extrahepatic cholestasis undergoing PTCD were classified into three groups, depending on the bilirubin decrease rate at two weeks after PTCD. Serum and biliary esterified bile acids in each group were measured before PTCD and at 24 hours, 48 hours, 1 week, and 2 weeks after PTCD. Bile acids were measured by Okuyama's methods (HPLC), and esterified bile acids were calculated from the difference between samples treated with sulfatase or beta-glucuronidase for enzymatic hydrolysis and untreated samples measured at the same time. The following results were obtained. The percentages of biliary esterified bile acids in total bile acids were as follows: before PTCD, in the fair improvement group, sulfate (S) = 6.4 +/- 4.6% (mean +/- S.D.), glucuronide (G) = 11.7 +/- 9.0%; in the poor improvement group, S = 2.8 +/- 1.6%, G = 1.0 +/- 0.9% and at 24 hours after PTCD, in the fair group, S = 9.1 +/- 7.5%, G = 7.5 +/- 4.3%; in the poor group, S = 2.9 +/- 2.4%, G = 1.7 +/- 1.1%. The percentages of esterified bile acids in the fair group were higher than in the poor group, and significant differences were noted in G (p less than 0.05). Thus PTCD is expected to reduce jaundice in cases with high percentages of biliary esterified bile acids before and shortly after PTCD.
...
PMID:Change in serum and biliary esterified bile acids in patients with extrahepatic cholestasis during percutaneous transhepatic cholangiodrainage. 338 78

To distinguish lysosome populations of HeLa cells, acid phosphatase, beta-glucuronidase, arylsulfatase and esterase were demonstrated using various substrates and couplers with different fixations, pHs and inhibitors. The substrates chosen were for acid phosphatase, naphthol AS-BI phosphate with fast red violet LB at pH 4.6; for beta-glucuronidase, naphthol AS-BI beta-D-glucuronide with fast red violet LB at pH 4.4; for arylsulfatase, p-nitrocatechol sulfate, with lead as the capturing ion, at pH 4.8 and 5.6; and for esterase, naphthol AS-D acetate with fast blue BB at pH 6.5. In the azo-dye methods, the coupling was always simultaneous and results were satisfactory with unfixed cells. For optimal demonstration of arylsulfatase, cells were fixed in glutaraldehyde in 0.1 M cacodylate buffer pH 7.2, 2% for 24 hr or 6.25% for 2 hr, and washed for 1-9 days in 0.1 M veronal acetate buffer pH 7.2, 7.5% with respect to sucrose. Two groups of lysosomes were distinguished. One comprised small bodies, probably primary lysosomes, which lay in a cluster near the nucleus. They had quite stable membranes and were mostly acid phosphatase-positive. They sometimes contained beta-glucuronidase or esterase, but rarely arylsulfatase. The other group included all the acid hydrolase-positive bodies scattered throughout the rest of the cytoplasm. They were mostly larger, with more labile membranes, and contained beta-glucuronidase, esterase or arylsulfatase, but rarely acid phosphatase.
...
PMID:Acid hydrolases in HeLa cells: comparison of methods for light microscopy. 343 9

A method for the preparation of calibration curves for acetaminophen glucuronide (NAPAG) and acetaminophen sulfate (NAPAS) in rabbit urine without use of authentic compounds in high-performance liquid chromatography was examined. Rabbits were dosed intravenously with acetaminophen (NAPA, 30 mg/kg). Urine was collected and diluted. A plot of the peak area ratio of NAPAG to internal standard against NAPA concentration after the hydrolysis of diluted urine with beta-glucuronidase was linear and passed through the origin. A linear tendency was also observed in the plot of the peak area ratio of NAPAS to internal standard against NAPA concentration calculated by the difference between the peak area ratio of NAPA after the hydrolysis with beta-glucuronidase and that with beta-glucuronidase/arylsulfatase. Thus, once the calibration curve has been prepared following the enzyme hydrolysis of NAPAG and NAPAS, then the concentration of NAPAG and NAPAS in the sample solution can be calculated from the peak of NAPAG and NAPAS, respectively. The method is simple, and has the advantage that pure standards of the individual NAPA metabolites are not required.
...
PMID:A method for the preparation of calibration curves for acetaminophen glucuronide and acetaminophen sulfate in rabbit urine without use of authentic compounds in high-performance liquid chromatography. 344 75

The biliary excretion of the carcinogen 6-hydroxy-methylbenzo[a]pyrene was investigated in rats after i.p. administration. Mutagenicity of the parent compound and its biliary metabolites was tested in Ames Salmonella/microsome mutagenicity assay. Approximately 40% of the dose administered (0.25-0.5 mg/kg) to the rats was excreted in the bile within 6 h. 6-Hydroxymethylbenzo[a]pyrene was excreted primarily as water-soluble metabolites, including glucuronide and sulfate conjugates. Negligible quantities of unchanged 6-hydroxymethylbenzo[a]pyrene were excreted in the bile. In the presence of Aroclor-induced S9, 6-hydroxymethylbenzo[a]pyrene was a potent mutagen. The mutagenicity of bile from rats treated with 6-hydroxymethylbenzo[a]pyrene was variable in the absence of an activation system. However, the same bile samples were mutagenic in the presence of beta-glucuronidase and/or S9. These results indicate that biliary metabolites of 6-hydroxymethylbenzo[a]pyrene can be metabolically activated to mutagenic species.
...
PMID:Mutagenic activity of biliary metabolites of 6-hydroxymethylbenzo[a]pyrene. 351 4

Cell walls of intact yeast- and mycelial-phase Candida albicans B311 were extracted with different compounds: dithiothreitol, dithiothreitol with protease, dithiothreitol with lyticase, and dithiothreitol with protease followed by beta-glucuronidase with chitinase. Extracts were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot techniques. Dithiothreitol extracts contained the most satisfactory array of components for study. Analysis of these extracts demonstrated that the outer cell wall layers of Candida blastoconidia and germ tubes contained a complex array of polysaccharides, glycoproteins, and proteins. The proteins contributed to a latticework stabilized by covalent bonds that was important in determining the porosity of the outer cell wall layers. When equivalent weights were analyzed, mycelial-phase extract contained a more varied array of proteins than did yeast-phase extract. Only a portion of proteins in mycelial-phase extract elicited antibody responses in hyperimmunized rabbits or infected humans. A polysaccharide-rich, high-molecular-weight component (migrating at a position that would correspond to proteins having molecular weights of 235,000 to 250,000) and a protein component (molecular weight, 19,000) were readily demonstrable in the mycelial-phase extract but could not be identified in the yeast-phase extract.
...
PMID:Analysis of cell wall extracts of Candida albicans by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot techniques. 352 86

A receptor which recognizes glycoproteins bearing terminal mannose residues has been isolated from human placental membranes. Washed membranes were solubilized with buffer containing 1% Triton X-100 and applied to a mannose-Sepharose affinity column. The column was eluted with buffer containing 200 mM mannose and 1% cholate. The major protein eluted exhibited a molecular weight of 175 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The protein binds 125I-labeled mannosylated bovine serum albumin in a saturable fashion with a dissociation constant of 4 nM. Ligand binding is pH-dependent with maximal binding above pH 6.5. This binding can be inhibited with EDTA, mannose, fucose, mannan, beta-glucuronidase, and bovine serum albumin conjugated to fucose. Polyclonal antibodies generated against the mannose binding protein immunoprecipitate a single 175-kDa protein species from both surface-iodinated and biosynthetically labeled human monocyte-derived macrophages.
...
PMID:Isolation and characterization of a mannose-specific endocytosis receptor from human placenta. 361 Oct 70

Adult male Fisher 344 rats (190-220 g), were given an intravenous dose (10 mg/rat) of BHA. Pretreated and control rats received an intravenous dose of [G-3H] acetaminophen (25 mg/rat). Bile was collected prior to dosing and for 5-6 hours after dosing at varying time intervals. Separate aliquots of 0.2 ml were incubated with beta-glucuronidase and sulfatase, respectively. These incubation mixtures were then extracted and analyzed by reverse phase HPLC. In all cases control animals showed a greater deceleration in the biliary excretion of the water soluble metabolites when compared with pretreated animals. Increases in both glucuronide and sulfate elimination processes are assumed to be contributory, in part, to the overall effect of BHA on acetaminophen metabolism.
...
PMID:BHA (2(3)-tert-butyl-4-hydroxyanisole)-mediated modulation of acetaminophen phase II metabolism in vivo in Fisher 344 rats. 362 63


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---