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)

In this work the alterations of some acrosomal enzymes and gamma-GT were studied in diseases of the male genital tract. Thirty-two patients with vascular diseases, seven with inflammatory diseases and twenty-four controls were investigated. In all patients the sperm morphology was studied and the following enzymes were assayed: beta-glucuronidase, beta-galactosidase, beta-glucosidase and gamma-GT. In all patients with vascular and inflammatory diseases we found severe hypokinesis and decreased number of spermatozoa. The activity of all four enzymes in both pathological groups was decreased in comparison with the controls, and this decrease was significant for all enzymes in males with vascular diseases and for beta-galactosidase and beta-glucosidase in cases with inflammatory diseases. Our data show that the decrease of spermatozoal count was accompanied by a decreased enzyme activity. The role of decreased sperm plasma enzyme activity, the decreased production of spermatozoa and quantitative changes in structure and acrosome enzyme content are discussed.
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PMID:Enzymes and cytomorphological sperm alterations in some diseases of the male reproductive system. 613 94

Glycosidase activities in the adults and juveniles of the lung fluke Paragonimus ohirai and P. westermani adults were demonstrated histochemically. For comparative studies, histochemical examination was also made on the adults of the liver fluke Fasciola hepatica. The enzymes examined were N-acetyl-beta-glucosaminidase (EC 3.2.1.30), beta-glucuronidase (EC 3.2.1.31), beta-galactosidase (EC 3.2.1.23), alpha-glucosidase (EC 3.2.1.20) and beta-glucosidase (EC 3.2.1.21). The distribution of beta-glucosaminidase was similar in juveniles and adults. Strong reaction sites for the enzyme were the caecal brush border, tegument, subtegumental cells and tests. In contrast, no staining reaction occurred in the caeca of F. hepatica, although the tegument and parenchymal cells were weakly stained. beta-glucuronidase activity was associated only with the luminal surface of the caeca in the juveniles. However, luminal contents also appeared stained and this might suggest that the activity in the caeca is not endogenous. beta-galactosidase was localized in the caeca, sub-tegmental cells and tegument in both juveniles and adults. No reaction occurred for the other two enzymes, alpha- and beta-glucosidase.
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PMID:Histochemical studies of glycosidase activity in juveniles and adults of the lung fluke Paragonimus. 622 Feb 58

The condition for maximal activity (pH, buffer, saturating substrate concentration, range of linear relationships between enzyme activity versus incubation time, and versus enzyme concentration) in the fluorimetric assay of several glycohydrolases of lysosomal origin in human plasma and serum have been established. The following enzymes were studied: alpha-galactosidase, beta-galactosidase, beta-N-acetylglucosaminidase, beta-glucosidase, beta-glucuronidase, alpha-mannosidase, alpha-fucosidase. All examined enzymes turned out to be more or less unstable upon storage at 37 degrees C, 4 degrees c, and -20 degrees C in both serum and plasma. The only exceptions were beta-glucuronidase, which was stable in plasma and serum, and alpha-fucosidase which was stable only in plasma. Generally the degree of instability was greater in serum than in plasma. The levels of some enzymes (alpha-galactosidase, beta-galactosidase, beta-N-acetyl glucosaminidase, beta=glucuronidase) were markedly higher in serum than in plasma; conversely the levels of the same enzymes in "platelet free" serum equalled those in plasma. This stresses the necessity to use freshly prepared plasma for lysosomal glycohydrolase assay. Under the procedural conditions recommended for the assay the methods for the determination of lysosomal glycohydrolases in plasma appeared to be simple, sensitive and reproducible.
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PMID:Enzymes of lysosomal origin in human plasma and serum: assay conditions and parameters influencing the assay. 625 26

The enzyme activities of alpha-fucosidase (pH 4.0 and pH 5.5), alpha-galactosidase, beta-galactosidase, alpha-glucosidase (pH 4.5 and pH 6.0), beta-glucosidase, beta-glucuronidase, beta-hexosaminidase, and alpha-mannosidase (pH 4.5 and pH 5.5) were investigated in sera from cystic fibrosis (CF) patients. Several of these activities were significantly increased in sera from patients compared to age-matched control children. CF-patients in a more advanced stage of the disease had a tendency to higher values of some of these hydrolases than those in better condition. No new isoenzymes of these hydrolases were found. Only minor differences could be detected in the pH-profiles of alpha-mannosidase and acid phosphatase from age-matched normal controls, heterozygotes and homozygotes for CF. With our technique, alpha-mannosidase and acid phosphatase showed the same thermostability in CF-patients. CF-heterozygotes and age-matched controls, except at 56 degrees C, when the activity of acid-phosphatase in the plasma from adult CF-heterozygotes decreased more than that from adult controls
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PMID:Acid hydrolases in sera and plasma from patients with cystic fibrosis. 626 20

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


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