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 effect of Fusarium sporotrichiella v. sporotrichioides mycotoxin (sporofusarin) on the total and non-sedimentary supernatant activity of 13 marker-enzymes of subcellular particles (2 mitochondrial enzymes-cytochrome oxidase and malate dehydrogenase; 8 lysosomal enzymes -- acid phosphatase, acid RNAase, acid DNAase, arylsulphatases A and B, beta-N-acetylglucosaminidase, beta-glucuronidase, beta-galactosidase and beta-glucosidase; 2 microsomal enzymes -- glucose-6-phosphatase and acetylesterase; plasma membrane enzyme -- alkaline phosphatase) of the rat liver, kidney, spleen and bone-marrow was studied in in vivo experiments. The latter demonstrated that sporofusarin effects were characterized by a significant organ and organella specificity, viz. the toxin caused a sharply increased activity, mainly of lysosomes enzymes and labilization of the lysosomal membranes, primarily in the spleen and the bone-marrow. A conclusion is drawn that the discovered selective destructive action of sporofusarin on the lysosomes may be regarded as a new phenomenon that, possibly is directly related to the characterization of the mechanism responsible for a specific effect produced by sporofusarin.
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PMID:[Lysosomal component in the mechanism of the toxic effect of sporofusarin]. 94 27

We studied the effect of diet on the activities of four enzymes found in the intestinal flora of the male F344 rat. Animals initially fed a diet with high vegetable and grain content were shifted to a diet consisting predominantly of beef. While eating the meat diet, the rats had significantly higher levels of nitroreductase, azoreductase, and beta-glucuronidase in their fecal flora when compared to levels measured during grain feeding. However, beta-glucosidase activity was significantly lower during meat feeding, which probably reflected the lack of beta-glucosidic linkages in this diet. These findings suggested that a high-beef diet, similar in composition to that consumed by humans with a relatively high risk of colon cancer, is associated with elevated levels of specific enzymes in the colon microflora. These enzymes have been implicated in the conversion of procarcinogens into carcinogens.
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PMID:The relationship between diet and rat fecal bacterial enzymes implicated in colon cancer. 100 18

The effect of the mycotoxin of Fusarium sporotrichiella v. sporotrichioides (sporofusarin) was studied in vitro on the total and nonsedimenting activity of eight lysosomal enzymes: acid ribonuclease, aryl sulfatases A and B, beta-glucuronidase, alpha- and beta-galactosidases, beta-glucosidase, beta-acetylglucosaminidase, and alpha-mannosidase. Incubation of a suspension of rat liver lysosomes with an aqueous solution of sporofusarin led to inhibition of the total activity of the membrane-bound lysosomal enzyme beta-glucosidase. In a dose of only 1.6 x 10-5 M sporofusarin caused a significant increase in the nonsedimenting activity of nearly all the enzymes; in a concentration of 1.6 x 10-3 M most of the enzymes of the lysosomal matrix (beta-glucuronidase, beta-galactosidase, aryl sulfatases A and B) were liberated almost completely into the supernatant, and nearly all the beta-glucosidase also was liberated. It is postulated that damage to the subcellular membranes is an important component of the toxic action of sporofusarin.
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PMID:Action of the mycotoxin of Fusarium sporotrichiella v. sporotrichioides on lysosomal membranes. 111 54

Effect of different concentration of non-ionic detergents (Triton X-100, Triton X-305, BRIJ-35 and Triton WR-1339) on total and non-sedimentable activity of 8 rat liver lysosome enzymes (acid phosphatase, acid DNase, acid RNase, arylsulphatases A and B, beta-glucuronidase, beta-galactosidase, beta-glucosidase and beta-acetylglucosaminidase) was studied. Only Triton X-100 at the concentration of 0.1% (and higher) was found to release completely lysosome enzymes. Low concentrations of Triton X-100 (0.025-0.05%) were used to characterize the strength of enzyme binding: the level of releasing acid DNase, beta-galactosidase, beta-glucuronidase and acid phsophatase being considerably higher than that of other lysosome enzymes studied. On the basis of the data obtained a method is worked out, which is suitable for series studies of the stability of lysosome membranes under different physiological and pathological conditions. The essence of the method is the treatment of membrane particles with increasing concentrations of Triton X-100 (0.025; 0.05 AND 0.1%) AND THE SUCCESSIVE ESTIMATION OF NON-Sedimentable activity of marker enzymes. The method detected troubles in the stability of rat liver lysosome membranes under starvation, protein deficiency and aging.
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PMID:[Determination of lysosome membrane stability]. 120 72

Effect of ethanol on functional activity of isolated perfused rat liver was studied (rate of O2 utilization, absorption of bromosulpholeine from perfusate, bile formation); total activity and activity in supernatant of nine marker enzymes were also determined (malate dehydrogenase, beta-glucuronidase, arylsulphatases A and B, beta-galactosidase, beta-glucosidase, acetylesterase, glucoso-6-phosphatase, alanine aminotransferase and aspartate aminotransferase). Activity of the enzymes was simultaneously studied in perfusate. Ethanol (0.5%) caused distinct impairement in functional activity of isolated liver; rate of bile formation and absorption of bromosulpholeine from perfusate were primarily altered. Degree of impairements in functional activity of liver tissue correlated with the concentration of ethanol in perfusate. In analysis of correlation between the total activity of the enzymes in liver tissue and their activity in supernatants and perfusate it was shown that the concentration (1%) of ethanol used did not produce damaye effect on plasma membranes and membranes of subcellular structures of hepatocytes, but, within certain limits, it displayed a stabilizing effect.
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PMID:[Effect of ethanol on stability of cell membranes in experiments using isolated liver]. 121 Jan 8

By means of isopycnic centrifugation in the continuous density gradient of sucrose two subfractions of lysosomes were isolated from rat liver homogenates: a "light" one (with the floating density p=1.13) and a "heavy" one (p=1.24). Electron microscopic, enzymatic and electron microscope enzymatic analysis of the isolated subfractions showed that the "light" subfraction consisted mainly of newly-formed primary lysosomes, while the "heavy" one was presented by secondary lysosomes. Parallel biochemical investigations demonstrated a considerable enzymatic heterogeneity of the two lysosomal subfractions: the "light" subfraction was characterized by a high specific activity of acid DNase, acid RNase and beta-galactosidase, and by almost total absence of beta-glucosidase activity, while the "heavy" one was characterized by a high specific activity of beta-glucosidase, beta-glucuronidase and beta-N-acetylglucosaminidase. Possible causes of enzyme heterogeneity of rat liver lysosomes are discussed.
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PMID:[Morphologic and biochemical heterogeneity of lysosomes]. 123 Oct 99

Human gallbladder epithelium was homogenized with a view to maintaining the integrity of subcellular components. In such homogenates, N-acetyl-beta-glucosaminidase, beta-glucuronidase, beta-galactosidase, beta-glucosidase, beta-fucosidase, beta-xylosidase, and acid phosphatase were demonstrated together with phospholipase activity. All the enzymes exhibited structure-linked latency. After discarding cellular debris from the homogenate, remaining subcellular organelles were analytically separated by density gradient centrifugation. After 100,000 g for 1 hour, particles containing acid glycosidases were recovered at a sucrose density of 1.18-1.19, whereas the mitochondrial marker enzyme succinate-reductase accumulated at a density of 1.16. The bulk of sedimentable phospholipase activity was recovered with particles sedimenting at 1.18-1.19. The results are interpreted as indicating that phosphalipase is present in lysosomes of the human gallbladder epithelium. Release of acid hydrolases, in lysosomes of the human gallbladder epithelium. Release of acid hydrolases, in lysosomes of the human gallbladder epithelium. Release of acid hydrolases, particularly phospholipase A, from the gallbladder epithelium is discussed as mediation of an inflammatory reaction in the gallbladder, i.e. cholecystitis.
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PMID:On the mediation inflammatory reaction in the human gallbladder epithelium. 127 7

Several lysosomal enzymes present in human plasma (N-acetyl-beta-glucosaminidase, beta-glucuronidase, beta-galactosidase, alpha-galactosidase, alpha-L-fucosidase, alpha-mannosidase, beta-glucosidase) were maintained in a fully active state for at least 8 months by the addition of ethylene glycol (300 milligrams final concentration) to freshly prepared plasma and storage at -20 degrees C. Pools of human plasma from healthy humans, stabilized and stored as above, and containing a low, medium or high content of the above enzymes, were used to establish the analytical imprecision (within-run, day-to-day and total imprecision) of the fluorimetric assay. Ten replicates in ten different analytical series, covering a period of two months, were performed. The total imprecision (expressed as coefficient of variation) was in general lower than 10%; in a few cases, particularly plasma samples with a low enzyme content, the total imprecision was 18%. The isozymes A, B, I1, and I2 of N-acetyl-beta-glucosaminidase displayed the same stability upon storage as the unfractionated enzyme. It is concluded that pools of human plasma containing known amounts of lysosomal enzymes, stabilized by the addition of 300 micrograms ethylene glycol and stored at -20 degrees C, are suitable liquid materials for calibration and quality control for the assay of the same enzymes.
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PMID:Preparation of a stable liquid material for calibration and quality control for lysosomal enzymes in plasma. Assay of enzymes of lysosomal origin in plasma, I. 133 72

The effects of dietary fat and dietary fiber (DF) levels in diet on fecal flora, activities of three fecal enzymes, putrefactive metabolites, fecal mutagenicity and fecal properties were studied in eight healthy volunteers. They were given low fat and low DF diet (LF: fat energy ratio was 13.9%, and DF intake was 9.0 g/day) for 10 days, high fat and low DF diet (HF: fat energy ratio was 52.7%, and DF intake was 7.1 g/day) for 10 days, and high fat and high DF diet (HFF: fat energy ratio was 52.0%, and DF intake was 24.8 g/day) for 10 days. No change of fecal flora at the bacterial group level was observed throughout the experimental period, except that the population of lactobacilli showed a tendency to increase in HF period. Fecal activities of beta-glucuronidase, beta-glucosidase and nitroreductase and some putrefactive products were unchanged between LF and HF, while these values decreased in HFF period. No significant change of fecal properties was observed between LF and HF, while by HFF supplementation fecal weight increased and fecal pH value was lower than that in LF and HF. Excretions of iron, zinc and calcium in feces did not increase by high DF supplementation.
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PMID:Effect of dietary fat and fiber on fecal flora, bacterial metabolites, and fecal properties in Japanese volunteers. 133 9

Gastric mucosal PG E2 receptors are the common antisecretory working point of all prostanoid types and may also be involved in "protective" effects. We investigated the subcellular localization of these receptors, as measured by displaceable 3H-PG E2 binding, and identified different organelles by monitoring the activities of specific marker enzymes. Porcine mucosal homogenates were subdivided by differential centrifugation into fractions P1 (1000 x g), P2 (20,000 x g), P3 (300,000 x g) and the supernatant S1. P3 was further fractionated over a series of sucrose step gradients. Mitochondria and lysosomes were enriched in P2 (maximum specific activities of cytochrome-c-oxidase of beta-glucosidase, beta-glucuronidase, beta-galactosidase, respectively). Plasma membranes (alkaline phosphatase, gamma-glutamyl-transpeptidase, 5-nucleotidase), tubulovesicles (H+/K(+)-ATPase) and rough endoplasmic reticulum (NADPH-cytochrome-c-reductase) were mainly found in P3, which also contained the majority of 3H-PG E2 binding sites. In contrast, prostanoid binding was barely detectable in S1. Density fractionation of P3 revealed that 3H-PG E2 binding sites shared a similar sedimentation profile with plasma membranes and tubulovesicular markers. No or negative correlation was found with lysosomes, rough endoplasmic reticulum and mitochondria. We conclude that mucosal PG E2 receptors are predominantly located at the cell surface. This supports the view that prostanoids inhibit gastric secretion through membrane receptors, but gives no clue for intracellular "protective" working points.
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PMID:Subcellular localization of prostaglandin E2 receptors in the gastric mucosa. 134 83


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