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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 objectives of this study were to determine the LC50 of methyl bromide (MeBr) and the dose-response curve and to study the detoxication effect of reduced glutathione (GSH) on MeBr poisoning in mice. 1) The LC50 of 4-h exposure to MeBr was 405 ppm in male mice with 95% confidence limits of 386-425 ppm. 2) The mortality rates of mice exposed to 500 ppm MeBr for 105, 120, 130, 140, 150 and 180 min were 0, 0, 10.7, 15.0, 85.0 and 90.0%, respectively. 3) In contrast, the mortality rate of mice pretreated with GSH (i.p 500 mg/kg; GSH-group) was only 5.3% after exposure to 500 ppm MeBr for 150 min. 4) Metabolic substances (Br-, GSH, formaldehyde, formic acid and
beta-glucuronidase
) were analyzed after exposure to 500 ppm MeBr and compared with the GSH-group and the distilled
water
treated group (DW-group). Except for GSH, concentrations of all other substances were significantly lower in the GSH-group than in the DW-group. Erythrocyte osmotic fragility test showed a significant increase in fragility in the DW-group. These results suggested that the onset of symptoms or death due to MeBr poisoning suddenly occurs at some point of concentration and time exposure. It was also shown that pretreatment with GSH effectively reduced mortality due to MeBr exposure.
...
PMID:[Experimental study on methyl bromide poisoning in mice. Acute inhalation study and the effect of glutathione as an antidote]. 202 Jan 25
Using a protein isolated from soy, a dynamic
water
adsorption method was developed and the data were compared with those obtained from a static gravimetric procedure. Both methods gave comparable results, showing that Type II isotherms with considerable hysteresis were obtained. However, the dynamic procedure was preferred since it provided data rapidly and used significantly less material. Using the dynamic method,
water
adsorption isotherms at 25 degrees C were also determined for four biologically active proteins: alpha-amylase,
beta-glucuronidase
, lipase, and urease. BET (Brunauer, Emmet, and Teller) parameters were calculated and the specific surface areas for the native, biologically active proteins were found to be similar, 238.4 +/- 20.2 m2/g. On the other hand, the specific surface area for the denatured soy protein isolate was 144.6 m2/g. Nevertheless, the heat of absorbance for all of the proteins examined was similar, suggesting that they have comparable degrees of hydrophilicity.
...
PMID:Water vapor adsorption and desorption isotherms of biologically active proteins. 202 66
In order to test the usefulness of BRILA-MUG (= Fluorocult) medium (Merck) for isolation and identification of total coliforms and faecal coliforms in surface
water
according to the EC guidelines for bathing waters a total of 969 strains of different Enterobacteriaceae and Vibrionaceae species was examined under different culture conditions. These included 486 E. coli (reference strains of O-groups 1-170, enterotoxin and Verotoxin-producing strains), 149 Salmonella (subspecies I-VI), 92 Yersinia, 44 Shigella, 64 Vibrio, 16 Aeromonas, and 118 strains of other Enterobacteriaceae species. After 48 h incubation at 36 degrees C 372 (82.0%) of 486 E. coli showed the typical reactions of gas formation, fluorescence (
beta-glucuronidase
activity), and indole production. Examination of fluorescence after addition of 1 N NaOH (0.5 ml), or testing of indole production after subculture in tryptophane containing broth improved the amount of typical reactions to 434 (95.4%). Incubation at 44 degrees C for 48 h gave less favourable results as compared with that at 36 degrees C. Out of 483 strains of other species 3.9% Salmonella strains of subspecies II-IV, 6.25% Citrobacter freundii, and 50% Edwardsiella tarda strains yielded reactions typical of E. coli. Shigella and Yersinia strains occasionally produced indole or fluorescence, but never visible gas.
...
PMID:[Reactions of different Enterobacteriaceae and Vibrionaceae species in BRILA-MUG (Fluorocult) bouillion]. 208 Sep 70
We examined the effectiveness of fluorogen in detecting bacterial enzymes in atypical or injured coliform strains in environmental
water
samples. 4-methylumbelliferyl-beta-D-galactoside and 4-methylumbelliferyl-beta-D-glucuronide, substrates for beta-galactosidase and
beta-glucuronidase
respectively, were used as markers for total and faecal coliform bacteria and it was confirmed that fluorogenic assays have a greater sensitivity than reference methods. It was also observed that adding MU-conjugates (50 micrograms/ml) to low selective media for membrane filtration, besides shortening test times, reduces false negative results when detecting sanitary microbial indicators of
water
pollution.
...
PMID:Fluorogenic detection of atypical coliforms from water samples. 211 78
This investigation studied the effects of a shift from a mixed diet to a lactovegetarian diet on some cancer-associated bacterial enzymes in human feces (
beta-glucuronidase
, beta-glucosidase, and sulphatase). Three months after the shift to the lactovegetarian diet, there was a significant decrease in
beta-glucuronidase
, beta-glucosidase, and sulphatase activities per gram feces wet weight (p less than 0.05, less than 0.05, and less than 0.001, respectively). In contrast, glucuronide and glucoside hydrolysis remained unchanged per gram dry weight, although sulphatase activity was still significantly lowered when expressed this way (p less than 0.01). However, the fecal excretion increased significantly (p less than 0.05). Part of the explanation for the decreased enzyme activities is obviously a dilution effect, because much of the increased fecal weight after the shift in diet was associated with a higher
water
content. The higher
water
content was probably due to a higher fiber intake (p less than 0.001). Thus, the results in this paper indicate that a change from a mixed diet to a lactovegetarian diet leads to a decrease in certain enzyme activities proposed to be risk factors for colon cancer.
...
PMID:Shift from a mixed diet to a lactovegetarian diet: influence on some cancer-associated intestinal bacterial enzyme activities. 212 19
The inhibitory effect of a protein isolated from rat serum on lysosomal acid cholesteryl ester hydrolase (acid CEH; EC.3.1.1.13) activity was studied. An inhibitor was purified from rat serum following ultracentrifugation and heat treatment using column chromatography on Sephacryl S-200 and ultrafiltration. The purified inhibitor appeared as a single protein band in sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. The molecular weight of the inhibitor was 28,000 Daltons as judged by gel filtration on Sephacryl S-200 and SDS-polyacrylamide gel electrophoresis. The purified inhibitor was shown to be apolipoprotein A-I (apo A-I), the major apolipoprotein of high-density lipoprotein (HDL), using immunoprecipitation with rat anti-apo A-I immunoglobulin (Ig)G. Inhibition of acid CEH activity by apo A-I was dependent on the concentration of apo A-I. The values of Vmax obtained were similar with or without apo A-I. Apo A-I of various other mammalian species, including human, bovine and rabbit, also inhibited acid CEH activity. Other apolipoproteins, such as apo A-II and apo B, also showed inhibiting activity. On the other hand, apo A-I had no effect on the activity of other enzymes found in lysosomes, such as cathepsin D,
beta-glucuronidase
and acid phosphatase. The results suggest that apolipoproteins may play a role in the regulation of hydrolysis of cholesteryl esters in lipoproteins, that have been transferred to the liver, and that the inhibition of acid CEH activity by apo A-I may be a characteristic of the lipid-binding protein or be due to changes of the lipid/
water
interface.
...
PMID:Properties of an acid cholesteryl ester hydrolase inhibitor from rat serum. 212 53
Gallbladder tissue from patients with acute acalculous cholecystitis contains increased amounts of prostanoids when compared to normal gallbladder tissue. Platelet-activating factor (PAF) is a potent stimulus of eicosanoid formation. It has been implicated as a mediator of acute inflammatory processes and systemic responses to shock. In this study the role of PAF in acute acalculous cholecystitis was evaluated. Anesthetized cats underwent gallbladder perfusion with a physiologic buffer solution containing [14C]polyethylene glycol as a nonabsorbable tracer to quantitate mucosal
water
absorption. Platelet-activating factor was infused into the hepatic artery for 2 hours. Control experiments were performed when vehicle alone was infused. Experiments also were performed when indomethacin was administered intravenously and when indomethacin and PAF were administered. Gallbladder mucosal absorption/secretion and perfusate and tissue prostaglandin E (PGE) and 6 keto prostaglandin F1 alpha (6-keto PGF1 alpha) levels were evaluated. Gallbladder inflammation was evaluated by
beta-glucuronidase
and myeloperoxidase tissue concentrations and by a histologic scoring system. Platelet-activating factor eliminated gallbladder absorption and produced net fluid secretion associated with dose-related increases in perfusate PGE concentrations and gallbladder tissue PGE and 6 keto PGF1 alpha levels when compared to control values. Platelet-activating factor produced significant inflammation in the gallbladder with increases in the histologic score of inflammation and tissue lysosomal enzyme activities. Indomethacin significantly decreased the fluid secretion, prostanoid levels, and inflammation produced by PAF. The results suggest that PAF may induce acute gallbladder inflammation associated with systemic stress through a prostanoid-mediated mechanism.
...
PMID:The role of prostanoids in the production of acute acalculous cholecystitis by platelet-activating factor. 217 43
In 1976, Kilian and Bulow described the association of
beta-glucuronidase
with the genus Escherichia (97% positive) and suggested that a
beta-glucuronidase
assay would be a useful identification test. Since that report, papers about the sensitivity and specificity of this enzyme for the identification of Escherichia coli from clinical sources, food, seawater, potable-
water
supplies, and various environmental sources have appeared. A study was undertaken to determine the efficacy and specificity of the defined-substrate technology
beta-glucuronidase
(Colilert) assay for the identification of this species from fecal samples. A total of 460 human, 105 cow, and 55 horse E. coli isolates were tested. Results showed 95.5%
beta-glucuronidase
-positive isolates in 24 h and 99.5% positive after 28 h of incubation. Only one E. coli isolate was negative. There were no significant differences in the percentage of
beta-glucuronidase
-positive isolates among the human or animal isolates. There were no non-E. coli isolates that were positive. All subjects carried
beta-glucuronidase
-positive E. coli.
...
PMID:Efficacy of beta-glucuronidase assay for identification of Escherichia coli by the defined-substrate technology. 218 9
A medium containing a chromogenic substrate was developed for the enumeration of Escherichia coli on the basis of
beta-glucuronidase
activity. In this medium there was an inverse linear relationship between the log initial E. coli concentration and the time taken for the color to reach a threshold optical density of 0.05. This relationship applied even when the E. coli population contained 5%
beta-glucuronidase
-negative cells. Incubation at 44 degrees C reduced the time taken for color development and allowed the procedure to be used in the presence of a competitive microflora that outnumbered the E. coli population by a factor of 10(4). Sodium lauryl sulfate as an additional selective agent gave no significant improvement. In the analysis of environmental
water
samples, the technique gave a good correlation with a standard cultural method. The procedure shows promise as a simple method for testing the compliance of environmental samples with microbiological criteria for E. coli.
...
PMID:Colorimetric enumeration of Escherichia coli based on beta-glucuronidase activity. 220 52
Since the biotransformation of paracetamol (Acetaminophen) is practically confined to conjugation, the quantitative determination of paracetamol excretion may provide important information on phase II of the drug metabolism. We elaborated a simple and rapid liquid chromatographic method for the assessment of paracetamol and its conjugated metabolites in the urine to be available for routine use in the clinicopharmacological laboratory. The persons involved in the trial were administrated 500 mg of paracetamol to be taken on an empty stomach in the morning. Subsequently, their urine was collected for 8 hours. The so-called free paracetamol of unchanged form excreted into the urine was measured from this 0 to 8 hours' urine fraction, then, after treating it with
beta-glucuronidase
/arysulphatase enzyme, the total amount of paracetamol released from the conjugate, as well as that of the existing free paracetamol, the so-called total paracetamol were determined. The urine extracts containing paracetamol obtained by ethylacetate, at pH 10, and dried under nitrogen stream were analysed by HPLC on an ODS column in an eluent of methanol and
water
mixture (3:7, v/v) in the presence of 3-acetaminophenol internal standard. The flow rate was 1 ml/min, the detection wavelength was 254 nm.
...
PMID:[Determination of paracetamol in urine by liquid chromatography]. 223 43
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