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)

A fibre-free diet, or the same diet supplemented with 100 g cabbage or carrot cell-wall preparation/kg, was fed to rats for 28 days and the activities of a number of caecal microbial enzymes (azoreductase, aryl nitroreductase, beta-glucosidase, beta-glucuronidase, imidazole nitroreductase and nitrite reductase) were determined in vitro. The plant cell-wall preparations diluted the gut contents and decreased the number of bacteria per gram of caecal contents. Enzyme activities per gram of caecal contents were also decreased, with the exception of beta-glucosidase activity which was significantly increased. These plant cell-wall preparations also increased caecal size, and thereby significantly increased total activity per caecum of microbial azoreductase, aryl nitroreductase, beta-glucosidase and beta-glucuronidase. When bacterial metabolism was expressed per 10(9) bacteria, all enzyme activities were significantly increased in caecal samples from rats fed the plant cell-wall preparations. There was an overall concordance of 0.91 between all the enzymes when expressed per 10(9) bacteria, but of only 0.38 when enzyme activities were expressed per gram of caecal contents.
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PMID:Metabolic profile of caecal micro-organisms from rats fed indigestible plant cell-wall components. 629 83

Rats, mice, and hamsters were fed a fiber-free purified diet for 30 days and the activity of a number of cecal microbial enzymes was determined. Expressed per gram cecal content, azoreductase activity was greatest in preparations from the hamster and least from the mouse, and beta-glucosidase and beta-glucuronidase activities were least active from the rat. Nitroreductase was less active and nitrate reductase more active from the hamster in comparison to the other species. When expressed per kilogram body weight, bacterial activities were always greatest from the hamster. When the basal diet was supplemented with pectin (50 g/kg diet), nitrate reductase activity was increased six- to sevenfold per gram cecal content for rats and mice (tenfold when expressed per kilogram body weight), but there was no effect on the nitrate reductase activity of hamster microflora. Pectin also significantly increased beta-glucuronidase activity in rats, but significantly reduced the activities of the other enzymes in at least one of the three species.
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PMID:A comparison of the activity of five microbial enzymes in cecal content from rats, mice, and hamsters, and response to dietary pectin. 630 41

Alpha-cellulose, added to a purified diet at six levels [0%, 2.5%, 5%, 10%, 20%, and 40% (w/w)] and fed to weanling rats for 3 weeks, had no effect on body weight, but it increased the weight of caecal contents and decreased the numbers of bacteria per total caecal contents. Caecal microbial azoreductase, nitroreductase, beta-glucosidase and nitrate reductase activities per total caecal contents were also significantly decreased by 10% dietary cellulose and above, yet beta-glucuronidase activity was only affected significantly by 40% dietary cellulose. Azoreductase and nitroreductase activities were highly correlated with one another and showed a similar response to cellulose.
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PMID:Effect of dietary cellulose on the metabolic activity of the rat caecal microflora. 630 19

Castanospermine (1,6,7,8-tetrahydroxyoctahydroindolizine) was tested against a variety of commercially available glycosidases and found to be a potent inhibitor of almond emulsin beta-glucosidase, and also to inhibit fungal beta-xylosidase. This alkaloid was inactive on yeast alpha-glucosidase, alpha- or beta-galactosidase, alpha-mannosidase, beta-N-acetylhexosaminidase, beta-glucuronidase, alpha-L-fucosidase. Fifty-percent inhibition of beta-glucosidase required about 10 micrograms/ml of castanospermine. The amount of inhibition was uniform throughout the time course, and the inhibition with regard to substrate concentration (p-nitrophenyl-beta-D-glucopyranoside) appeared to be of the mixed type. Castanospermine was also a potent inhibitor of beta-glucocerebrosidase when assayed with fibroblast extracts using either a fluorimetric or a radioactive assay. Interestingly enough, castanospermine also inhibited the lysosomal alpha-glucosidase, and this inhibition required comparable levels of alkaloid to that required for inhibition of beta-glucocerebrosidase. However, a number of other lysosomal glycosidases were not sensitive to castanospermine (i.e., alpha- or beta-galactosidase, alpha- or beta-mannosidase, alpha- or beta-L-fucosidase, beta-N-acetylhexosaminidase, beta-glucuronidase).
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PMID:Castanospermine, a tetrahydroxylated alkaloid that inhibits beta-glucosidase and beta-glucocerebrosidase. 640 22

The effect of in vitro capacitation (events that occur before the acrosome reaction) on the acrosomal enzymes of human spermatozoa was determined. Capacitation of human spermatozoa was assessed by their ability to penetrate denuded hamster oocytes. The activities of a number of enzymes commonly associated with the sperm acrosome, including nonzymogen acrosin, proacrosin, inhibitor-bound acrosin, hyaluronidase, acid phosphatase, beta-glucuronidase, beta-glucosidase, beta-N-acetylglucosaminidase, beta-galactosidase and beta-N-acetylgalactosaminidase were assessed. With the exception of acid phosphatase, no alteration in enzyme activity occurred after 4 h of incubating the spermatozoa under capacitation conditions although gamete fusion took place. The acid phosphatase levels decreased twofold, presumably due to the loss of seminal (prostatic acid phosphatase that loosely adheres to spermatozoa. After 8 h of capacitation, a large decrease in sperm enzyme levels took place only in the case of hyaluronidase, although small decreases were also noted in total acrosin, proacrosin and inhibited acrosin. No new electrophoretically migrating forms of acrosin were observed. Decreases in total acrosin and proacrosin, but not in inhibited acrosin, also occurred when spermatozoa were incubated under noncapacitating conditions for 8 h, indicating that capacitation may specifically cause the release of some acrosin inhibitor from human spermatozoa. It is concluded that, with the possible exception of hyaluronidase, the in vitro capacitation of human spermatozoa does not cause a major change in its acrosomal enzyme content so that these hydrolases are fully present before the acrosome reaction takes place during gamete fusion. Serum albumin appears to protect against the loss of some of these enzymes since the activity of several glycosidases was significantly reduced when the spermatozoa were incubated for 8 h in human serum albumin-free medium.
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PMID:Acrosomal enzymes of human spermatozoa before and after in vitro capacitation. 640 71

The enzyme activity of the rat hindgut microflora maintained in an anaerobic two-stage continuous culture was compared with that of rat cecal contents. A qualitative comparison (API ZYM) showed a high degree of similarity between the two populations. Quantitative determinations showed that azoreductase, beta-glucosidase, nitrate reductase, and nitroreductase activities were comparable, and that beta-glucuronidase activity was very low in the culture. beta-Glucuronidase, beta-glucosidase, and nitrate reductase activities were induced within the culture by their respective substrates. Bile acids influenced microbial activity in vitro, with cholic acid inducing beta-glucosidase, azoreductase, and beta-glucuronidase activities and decreasing nitrate reductase activity. Chenodeoxycholic acid increased beta-glucosidase and beta-glucuronidase activities and decreased azoreductase, nitrate reductase, and nitroreductase activities in vitro. These studies demonstrate that the rat hindgut microflora may be successfully cultured in vitro and suggest control mechanisms that regulate the metabolic activity of these organisms in vivo.
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PMID:Metabolic activity and enzyme induction in rat fecal microflora maintained in continuous culture. 641 66

Weanling or adult (9 wk old) rats were fed diets containing 0, 250 or 500 g lactose/kg for 10 days, after which the activities of six caecal microbial enzymes (azoreductase, beta-glucosidase, beta-glucuronidase, nitrate reductase, nitroreductase and urease) were determined. Adult controls had larger caeca than weanlings, but the numbers of bacteria were not significantly different. Expressed in relation to body weight, caecal microbial enzyme activities were significantly lower in adult controls, with the exceptions of beta-glucuronidase and urease. Lactose caused caecal enlargement; this was greatest in weanling animals, which also showed a decreased concentration of bacteria. Lactose increased total nitrate reductase and urease activities in both age groups, but decreased total azoreductase and nitroreductase activities in weanlings. Enzyme activities per 10(9) bacteria were decreased for azoreductase, beta-glucosidase, beta-glucuronidase and nitroreductase in both age groups, while urease activity increased. Azoreductase and nitroreductase activities were highly correlated but nitrate reductase and urease did not correlate significantly with any other enzyme activity.
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PMID:Dietary lactose and the metabolic activity of the caecal microfloras of weanling and adult rats. 642 83

Changes in the activities of several lysosomal enzymes were studied during transformation of mouse spleen cells in vitro. The activity of beta-glucuronidase increased during culture in the presence of T or B-cell mitogens, and lymphoblasts contained higher levels of activity than did small, non-transformed lymphocytes. Moreover, lymphoblasts in well-transformed cultures had higher activities than those in poorly-transformed cultures. The activities of other lysosomal enzymes (N-acetyl-beta-glucosaminidase, alpha-mannosidase, beta-glucosidase) also increased during mitogenic stimulation, but each at different rates, although aryl sulphatase was unaffected. Such differences may be of importance when lymphocytes are used for diagnosis of inherited lysosomal deficiency diseases.
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PMID:Effects of mitogenic stimulation of lymphocytes on lysosomal enzyme activity. 643 92

In platelets of subjects affected with myeloproliferative disorders the following lysosomal enzymes were studied: alpha-mannosidase, alpha-fucosidase, beta-galactosidase, beta-glucosidase, beta-glucuronidase, beta-N-acetylglucosaminidase and acid phosphatase. For each enzyme the specific activity, the optimum of pH and buffer, Km and saturating substrate concentrations, as well as thermostability were determined. Control and patient enzymes showed no difference.
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PMID:Platelet lysosomal enzymes are normal in myeloproliferative disorders. 643 83

Mouse peritoneal macrophages that had been treated with a monovalent carboxylic ionophore, monensin, selectively secreted lysosomal and nonlysosomal granular enzymes into the medium. When macrophages were incubated with 1 to 10 microM monensin, the release of beta-glucuronidase, beta-hexosaminidase and beta-galactosidase was stimulated time and does dependently. Neither the beta-glucosidase nor acid phosphatase, enzymes bound to the lysosomal membranes, however, were released by monensin. Neutral alpha-glucosidase, shown recently to be localized in nonlysosomal granules of macrophages (15), was released by monensin at concentrations lower than those required for lysosomal enzyme release. Increased release of lysosomal enzymes also took place in a manner similar to that seen with monensin-treated macrophages after treatment of macrophages with weak bases, chloroquine and ammonium chloride. Neutral alpha-glucosidase, however, was not released when chloroquine was present in concentrations that stimulated the release of lysosomal enzymes. The UDP-galactosyltransferase activity of the Golgi apparatus in the macrophages markedly decreased after treatment with low concentration of monensin.
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PMID:Stimulation of the release of lysosomal and nonlysosomal granular enzymes from macrophages treated with monensin. 643 21


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