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:3.2.1.26 (invertase)
4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mucosa from the duodenal and jejunal regions of pig small intestine was repeatedly freeze-thaw treated to solubilize an enzyme preparation, enriched in maltase, glucoamylase and alpha-limit dextrinase activities; isomaltase and sucrase remained essentially insoluble during the treatment. Chromatographic procedures, including ion-exchange, gel filtration and hydroxylapatite chromatography of the solubilized preparation, brought to homogeneity an alpha-glucosidase active towards maltose, alpha-limit dextrins and starch in decreasing order, with only a very weak capacity to hydrolyse alpha-1,6-linkages. Michaelis constants and maximal velocities, as well as relative rates of hydrolysis of several substrates, including maltodextrins and alpha-limit dextrins, were determined and served to characterize what seems to be a rather specific alpha-1,4-glucosidase. The participation of this enzyme in the hydrolysis of alpha-limit dextrins and more generally in pathways for starch breakdown in the pig digestive tract is examined and discussed.
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PMID:Purification and characterization of a pig intestinal alpha-limit dextrinase. 633 42

20 reference strains and 72 isolated strains from dental plaque of streptococci, actinomyces, and lactobacilli species were examined for sucrase and maltase activities. The type of sucrase in the different strains was determined by use of the alpha-glucosidase inhibitor, acarbose. The enzyme activities were determined as formation of monosaccharide, and quantitated spectrophotometrically. Although variations occurred in enzyme activities between reference and isolated strains, the same general pattern was noticed. Strains of Streptococcus mutans and S. salivarius showed regularly the highest sucrase activities, followed by strains of Actinomyces viscosus and A. naeslundii. Most lactobacilli belonged to the bacteria with low sucrase activity like S. sanguis and S. mitior. In some lactobacilli strains, however, a high sucrase activity was observed. The level of sucrase activity in S. mutans strains was dependent on biotype/serotype, as strains of biotype V/serotype e showed high activities, biotypes I and IV corresponding to serotypes c, f, and d showed intermediate activity, and biotype III/serotype a always showed low activity. In most of the strains the sucrases were composed of enzymes with specificity against both alpha-glucosidic linkage and beta-fructosidic linkage of the sucrose molecule, but in varying ratios. In all species, exept S. sanguis and S. mitior, lower maltase than sucrase activity was observed, but even in the two species mentioned the maltase activities were relatively low. On the basis of observations of selected reference strains in every species examined both sucrases and maltases are to some extent inducible.
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PMID:Sucrase and maltase activities in supragingival dental plaque in humans of streptococcal, actinomyces and lactobacilli species. 637 64

A naturally occurring enteropathy was identified in Irish setter dogs and wheat-sensitivity was demonstrated in a litter bred from two of the affected animals. The morphological and biochemical features of this enteropathy are described and compared to coeliac disease in man. Affected animals comprised 10 dogs that presented with poor weight gain or weight loss, with or without diarrhoea. Exocrine pancreatic function was normal and culture of duodenal juice demonstrated no marked bacterial overgrowth. Serum vitamin B12 concentrations were unaltered, but in some cases low serum and erythrocyte folate concentrations and reduced xylose absorption provided indirect evidence for proximal small intestinal disease. Examination of peroral jejunal biopsies revealed patchy morphological changes within individual animals, comprising predominantly partial, but in one case subtotal, villous atrophy. Brush border enzymes were selectively altered: the specific activities of alkaline phosphatase, leucyl-2-naphthylamidase and of zinc-resistant alpha-glucosidase were reduced by approximately 40 per cent, while activities of maltase, sucrase, lactase and gamma-glutamyl transferase were unaltered. Activity of a lysosomal enzyme was increased and there was evidence for enhanced lysosomal fragility. The activity of malate dehydrogenase, with a dual mitochondrial and cytoplasmic localisation, was decreased but there were no changes in the activities of marker enzymes for basal-lateral membranes, endoplasmic reticulum or peroxisomes. These findings, particularly the specific biochemical abnormalities, were comparable to those in partially treated coeliac disease in man; however, a specific role for wheat in the pathogenesis of the disease has yet to be defined.
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PMID:Morphological and biochemical studies of a naturally occurring enteropathy in the Irish setter dog: a comparison with coeliac disease in man. 652 28

To define reproducible conditions for the homogenization of small-intestinal biopsy samples, tissue homogenization has been studied by the use of three different homogenizers. Tissue samples of increasing wet weights (0.5-10.8 mg) were homogenized in a fixed volume (1 ml) before DNA and protein were determined. The DNA to protein ratio was calculated for all wet weights and used as a measure for reproducible homogenization. The minimum tissue wet weight needed for analysis (2 mg) was determined from the values obtained for the DNA to protein ratio. Highly sensitive techniques are described in detail for the assay of brush border (maltase, lactase, sucrase, neutral alpha-glucosidase, alkaline phosphatase, gamma-glutamyl transferase, leucyl-beta-naphthylamidase), basolateral membrane (5'-nucleotidase), and mitochondrial (succinate dehydrogenase) marker enzymes and for four acid hydrolases (acid phosphatase, acid beta-D-galactosidase, N-acetyl-beta-D-glucosaminidase, acid diesterase) in human and rat jejunal mucosa. Linear kinetics have been established for all enzyme assays. The optimal dilution of tissue homogenate for the assay of the various enzymes has been determined to enable the determination of a maximum number of enzymes in each homogenate. The range of enzyme activities in samples of human and rat jejunal mucosa has been determined.
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PMID:Enzyme activities in human and rat jejunal mucosa. 667 54

A series of marker enzymes for brush borders, basolateral membrane, and lysosomes were assayed in mucosal biopsy specimens from patients with untreated and treated coeliac disease and from controls. The brush border enzymes lactase, sucrase, neutral alpha-glucosidase, alkaline phosphatase, and leucyl-beta-naphthylamidase showed reduced activities in the untreated state and complete or partial normalization during treatment. The lysosomal marker enzyme acid phosphatase increased in activity in untreated coeliac disease and was normalized by treatment. The brush border enzyme gamma-glutamyl transferase was nearly normal in untreated patients and slightly increased in treated patients. The basolateral membrane marker, 5'-nucleotidase, was reduced both in untreated and treated patients, whereas the lysosomal marker N-acetyl-beta-glucosaminidase was normal in the untreated state and decreased during treatment. The possible pathogenetic role of the three latter enzymes in coeliac disease is discussed. The patterns of the other enzymes are suggested to be attributable to the morphologic changes in the mucosa.
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PMID:Jejunal mucosal enzymes in untreated and treated coeliac disease. 667 55

The subcellular biochemical features of a naturally occurring enteropathy in the dog associated with bacterial overgrowth have been examined. Affected animals comprised a group of 10 German Shepherd dogs with raised serum folate and reduced vitamin B12 concentrations, mild steatorrhoea, reduced xylose absorption, and normal exocrine pancreatic function. Culture of duodenal juice showed bacterial overgrowth with mixed flora, most frequently including enterococci and Escherichia coli. Examination of peroral jejunal biopsies revealed predominantly minimal histological but distinct biochemical abnormalities in the mucosa. The specific activity of alkaline phosphatase was decreased, isopycnic density gradient centrifugation showing a marked loss particularly of the brush border component of enzyme activity. In contrast, gamma-glutamyl transferase activity was enhanced in brush border fragments of slightly increased modal density, but there were no changes in the activities of the carbohydrases, zinc-resistant alpha-glucosidase, maltase, sucrase, and lactase or of the peptidase, leucyl-2-naphthylamidase. Activities of lysosomal enzymes were increased and there was evidence for enhanced lysosomal fragility and mitochondrial disruption. The activities and density gradient distributions of marker enzymes for basal-lateral membranes, endoplasmic reticulum and peroxisomes were essentially unaltered. These findings show that bacterial colonisation of the proximal small intestine may be associated with specific alterations in microvillus membrane proteins and provide biochemical evidence for intracellular damage to the enterocytes.
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PMID:Biochemical changes in the jejunal mucosa of dogs with a naturally occurring enteropathy associated with bacterial overgrowth. 674 19

Inhibition of microbial enzymes in human dental plaque catalyzing the cleavage of the disaccharides maltose, sucrose and lactose was carried out with the alpha-glucosidase inhibitor, acarbose. The maltases from plaque homogenates were totally inhibited, whereas the inhibition of the invertases varied considerably. With increasing inhibitor concentrations, from 1 mM to 50 mM, the inhibition of the invertases increased. Preincubation for 30 min of the plaque homogenate with inhibitor resulted in a 20% increase of the inhibition of invertase activity. The inhibitor showed non-competitive inhibition of the invertases in the homogenates, whereas the maltases were competitively inhibited. The lactases were not inhibited at all. The invertases from human dental plaque may be alpha-glucosidases and/or beta-fructosidases.
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PMID:Effect of the alpha-glucosidase inhibitor, acarbose, on disaccharide splitting enzymes in human dental plaque. 680 51

The toxicity to the cells and protoplasts of Saccharomyces cerevisiae of the sugar analogues modified at carbon 2 increases in the order 2-deoxy-D-glucose (DG), 2-deoxy-2-fluoro-D-glucose (FG) and 2-deoxy-2-fluoro-D-mannose (FM). The fluorohexoses, similarly as DG, behave generally as analogues of both glucose and mannose, depending on the hexose used as a carbon source in the medium. Relative inhibitions of glucan and mannan synthesis in protoplasts were found to be dependent more on glucose and mannose used as the growth support than on the type of the sugar analogue. Certain degree of structural relationship of fluorohexoses to the corresponding natural hexoses was reflected in their effects on growth of intact cells. Growth on glucose was inhibited most effectively by FM, growth on mannose by FG. The data obtained support the view that the sugar analogues interfere mainly with the glucose-mannose interconversion catalyzed by hexosephosphateisomerases. A comparison of the effects of fluorohexoses and DG on the synthesis of extracellular invertase an intracellular alpha-glucosidase and alkaline phosphatase in protoplasts pointed to the fact that all three sugar analogues tested also participate in metabolic control of enzyme synthesis.
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PMID:A comparison of the toxic effects of 2-deoxy-D-glucose and 2-deoxy-2-fluoro-D-hexoses on Saccharomyces cerevisiae cells and protoplasts. 703 85

The effect of concanavalin A on biosynthesis of nucleic acids, proteins, structural polysaccharides and glycoproteins of the yeast cell membrane and of enzymes having different localization in the cell as well as on other processes occurring in spheroplasts of the yeasts Saccharomyces cerevisiae IBPhM-350 and CCY 21-4-13 were studied. In both yeast strains lectin strongly inhibited total protein synthesis and produced a weaker inhibiting effect on DNA and RNA synthesis. This was accompanied by a decrease of the activity of the majority of already known enzymes (acid phosphatase, invertase, alpha-glucosidase, polyphosphatase, pyrophosphatase, ATPase) and glucose consumption. In addition concanavalin A inhibited the synthesis of structural components of the yeast cell membrane, i.e. mannane and glucane. The data obtained suggest that lectin (50 microgram/ml or higher) has a toxic effect on yeast spheroplasts (or protoplasts).
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PMID:[Inhibiting effect of concanavalin A on certain biosynthetic processes in spheroplasts of the yeast Saccharomyces cerevisiae]. 705 45

Doses of 3 mg/kg Ro 10-9359 (in arachis oil) were daily administered to adult female Wistar rats by gastric tube for a period of 10 days. Control animals received corresponding quantities of arachis oil only. The body weight of all rats was registered daily. Samples of jejunum and ileum were processed for quantitative histochemical analysis of neutral alpha-glucosidase kinetics and for three-dimensional evaluation of the mucosal architecture. In addition, mucosal scrapings were prepared from these intestinal segments, and the specific sucrase activity was determined. For each animal data were pooled and analyzed by Wilcoxon (Wn) test. Body weight and all registered parameters in the jejunum of treated animals remained unchanged as compared to the controls. In the ileum, however, we found under aromatic retinoid an increase of sucrase activity (P = 0.02) and of mucosal surface per unit serosal area (P less than 0.05). The hydrolytic activity of neutral alpha-glucosidase (Vmax) showed a clear trend to increase at both the villus base and apex, whereas the apparent substrate affinity (Km) remained unaltered. Our results show that, in closes of 3 mg/kg/day, aromatic retinoid induces (1) an increase in mucosal surface area, apparently due to hyperproliferation of the absorptive epithelium in ileum, which could facilitate its absorptive capacity and (2) an increase of specific sucrase activity, which could result in an enhanced carbohydrate assimilation. These findings indicate that Ro 10-9359 in addition to its effects on keratinizing epithelia exerts a distinct influence on the structure and function of the intestinal epithelium.
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PMID:Effects of aromatic retinoid on non-keratinizing (intestinal) epithelium: biochemical and morphological studies. 718 74


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