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 procedure was developed for the analytical isolation of brush border and basal lateral plasma membranes of intestinal epithelial cells. Brush border fragments were collected by low speed centrifugation, disrupted in hypertonic sorbitol, and subjected to density gradient centrifugation for separation of plasma membranes from nuclei and core material. Sucrase specific activity in the purified brush border plasma membranes was increased fortyfold with respect to the initial homogenate. Basal lateral membrane were harvested from the low speed supernatant and resolved from other subcellular components by equilibrium density gradient centrifugation. Recovery of Na, K-ATPase activity was 94%, and 61% of the recovered activity was present in a single symmetrical peak. The specific activity of Na, K-ATPase was increased twelvefold, and it was purified with respect to sucrase, succinic dehydrogenase, NADPH-cytochrome c reductase, nonspecific esterase, beta-glucuronidase, DNA, and RNA. The observed purification factors are comparable to results reported for other purification procedures, and the yield of Na, K-ATPase is greater by a factor of two than those reported for other procedures which produce no net increase in the Na, K-ATPase activity. Na, K-ATPase rich membranes are shown to originate from the basal lateral plasma membranes by the patterns of labeling that were produced when either isolated cells or everted gut sacs were incubated with the slowly permeating reagent 35S-p-(diazonium)-benzenesulfonic acid. In the former case subsequently purified Na, K-ATPase rich and sucrase rich membranes are labeled to the same extent, while in the latter there is a tenfold excess of label in the sucrase rich membranes. The plasma membrane fractions were in both cases more heavily labeled than intracellular protein. Alkaline phosphatase and calcium-stimulated ATPase were present at comparable levels on the two aspects of the epithelial cell plasma membrane, and 25% of the acid phosphatase activity was present on the basal lateral membrane, while it was absent from the brush border membrane. Less than 6% of the total Na, K-ATPase was present in brush border membranes.
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PMID:Analytical isolation of plasma membranes of intestinal epithelial cells: identification of Na, K-ATPase rich membranes and the distribution of enzyme activities. 13 16

The mucosal enzyme activities of 11 marker enzymes from the brush border, basolateral membrane, and lysosomes of 45 patients with an active duodenal ulcer (DU) were determined by analysis of homogenized biopsy specimens obtained from the duodenal bulb and descending duodenum at endoscopy. They were compared with activities measured in 22 controls. In the duodenal bulb lactase (p less than 0.005), neutral-alpha-glucosidase (p less than 0.0005), and monoamine oxidase (p less than 0.0005) were significantly decreased in DU patients. In the descending duodenum all the brush border enzymes except sucrase were significantly decreased when compared with controls. DU patients with inflammation in the biopsy specimens from the duodenal bulb had decreased levels of lactase (p less than 0.05), sucrase (p less than 0.05), neutral-alpha-glucosidase (p less than 0.05), leucyl-beta-naphthylamidase (p less than 0.05), and acid phosphatases (p less than 0.05) when compared with DU patients with normal histology in this region. In the descending duodenum the activities of leucyl-beta-naphthylamidase (p less than 0.05) were decreased in patients with inflammation compared with those without such histologic changes. DU patients who had taken antacids before the investigation had decreased activities of lactase (p less than 0.05) in the descending duodenum when compared with those who had not taken antacids. Activities of lactase (p less than 0.005), sucrase (p less than 0.005), neutral-alpha-glucosidase (p less than 0.05), and acid beta-glucuronidase (p less than 0.0005) in the descending duodenum were significantly lower in smokers than in non-smokers with active DU.
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PMID:Enzyme activities in the duodenal mucosa in duodenal ulcer patients. 292 38

A technique for the isolation of intact brush borders from rabbit renal cortex was evaluated. The procedure was monitored by phase and electron microscopy and marker enzymes, i.e. ATP:NMN adenylyl transferase, nuclear; cytochrome oxidase, mitochondrial; beta-glucuronidase, lysosomal; and glucose-6-Pase, microsomal; and indicated an essentially pure preparation of brush borders. The disaccharidase, trehalase, previously reported in renal tubules, was localized uniquely in brush borders. Maltase was also found; the specific activities of the two enzymes in the brush borders were increased 10- to 20-fold. Other disaccharidases, such as sucrase, isomaltase, lactase, and cellobiase, were absent. It is suggested that trehalase and maltase are appropriate candidates for marker enzymes of the renal brush border. Isolated brush borders possessed a ouabain-sensitive (Na(+) + K(+)) ATPase, an oligomycin-insensitive Mg(++) ATPase, and a Ca(++)-activated ATPase. Alkaline phosphatases, dephosphorylating beta-glycero-P, and trehalose-6-P were also present. The specific activities of these enzymes were increased three-to-five fold in the brush-border preparations; however, activities were found in other subcellular fractions of the renal cortex. Hexokinase, although evident in the isolated brush border, was found prominently associated with other membranous fractions. Phosphoglucomutase and UDPG pyrophosphorylase were localized in the soluble fraction of the renal cortex.
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PMID:Isolation and biochemical characterization of brush borders from rabbit kidney. 425 Jun 12

In a four-week experiment on 60 7-day-old BUT-9 male turkeys the effects of dietary fructooligosaccharides (pure nystose and a fructooligosaccharide mixture) supplemented at 1 and 2%, were studied on ileal and caecal metabolism. The control carbohydrate was cellulose, added also at 1 or 2%. Each dietary treatment consists of 10 birds kept individually. The average degree of polymerisation of the nystose and oligofructose preparation amounted to 2.9 and 4.1, respectively. The addition of nystose significantly decreased the pH value and viscosity in the ileal contents compared with the cellulose treatment. On the other hand, the oligofructose preparation increased the activity of sucrase and lactase in the ileal mucosal by 30-60% and 33-47%, respectively. Both fructan preparations similarly acidified the caecal and colonic digesta (by 0.2-0.4 pH units) as well as diminished the activity of bacterial harmful beta-glucuronidase (by 24-40%), but only nystose caused an enlargement of the caeca and effectively reduced caecal ammonia concentration, especially at a higher dose. Oligofructose supplementation at 2% caused a 3.5-fold increase of bacterial activity of alph- and beta-galactosidase, while 2% nystose resulted in 1.7 and 3 times higher alpha- and beta-glucosidases activities, respectively. Compared to oligofructose, dietary nystose increased propionic and decreased butyric fermentation in caeca. Nystose and oligofructose preparations added at 2% reduced the triacylglycerol concentration in the serum in comparison to the addition of 2% cellulose by 46 and 25%, respectively. Beside the fact that dietary levels of supplementation were of great importance, the results indicated that even small difference in the length of carbohydrate chain may cause different physiological responses.
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PMID:Gastrointestinal tract metabolism of young turkeys fed diets supplemented with pure nystose or a fructooligosaccharide mixture. 1894 86

An experiment was conducted to investigate the effects of diets containing soybean meal (SBM), soybean protein concentrate (SPC), and soybean protein isolate (SPI) on growth performance and gut function of the young turkey. A total of 812 one-day-old male turkey poults were randomly assigned to 4 dietary treatments, with 7 pens per treatment and 29 birds per pen. The 4 experimental diets contained SBM, SBM-SPC, SPC, and SPI and were fed throughout the two 4-wk experimental periods. In each period, the diets were isonitrogenous and isocaloric and contained similar amounts of total and water-soluble nonstarch polysaccharides. The content of oligosaccharides differed among the diets and averaged 2.4, 1.9, 0.9, and 0.1% for SBM, SBM-SPC, SPC, and SPI, respectively. When compared with SBM, birds consuming the SBM-SPC and SPC diets had higher (P<0.05) final BW (4.32 vs. 4.45 and 4.46 kg, respectively). Incorporation of SPI as a substitute for SBM resulted in improved (P<0.05) feed utilization (from 1.76 to 1.67) but did not affect the final BW. Significant changes in cecal concentrations of short-chain fatty acids were observed and averaged 130, 103, and 89 micromol/g of digesta for the SBM, SBM-SPC, and SPC diets, respectively. This coincided with the proportional decrease in dietary oligosaccharide content (from 2.4 to 0.9%) and was further substantiated by a significant decrease in ileum weights. Feeding the SPI diet resulted in the lowest ileal and cecal tissue weights as well as the lowest cecal short-chain fatty acids concentration. There was no effect of diet on digesta pH, viscosity, and mucosal sucrase and maltase activities. Bacterial beta-glucuronidase activity was decreased (P=0.08) in the cecum (from 0.98 to 0.60 U/g) with decreased dietary oligosaccharide content. In conclusion, partial or almost complete substitution of SBM with SPC suppressed the fermentation processes in the ceca but enhanced the growth rate. Substitution of SBM with SPI significantly improved feed utilization but decreased BW of 4-wk-old turkeys with no effect on growth rate of older 8-wk-old birds.
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PMID:The effect of diets containing soybean meal, soybean protein concentrate, and soybean protein isolate of different oligosaccharide content on growth performance and gut function of young turkeys. 1976 67