Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.20 (alpha-glucosidase)
 4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Dog enterocyte brush border proteins have been studied after a 75% proximal resection of the small bowel. This study was carried on microvillar membrane preparations purified from ileal mucosa sampled before and after regeneration on neighbouring intestinal segments, each animal acting as its own control. After six weeks of regeneration a statistically significant decrease of the following enzyme specific activities was observed: lactase, cellobiase, maltase, sucrase, palatinase, dextranase, trehalase, alkaline phosphatase, aminopeptidase and gamma-glutamyl transferase. Analysis of brush border proteins by polyacrylamide gel electrophoresis in presence of sodium dodecyl sulphate have shown after regeneration a decreased rate for the proteins with a molecular weight higher than 100,000 daltons. Modifications of electrophoretic patterns seem to be related to the specific activity decreases observed for brush border enzymes after regeneration, since the molecular weight of these enzymes were found between 116,000 and 285,000 daltons, after gel filtration.
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PMID:Effect of massive proximal small bowel resection on intestinal brush border membrane proteins in the dog. 8 27

1. The carbohydrase activities of homogenates of mucosa from the abomasum, small intestine, caecum and colon, and of the pancreas of cattle were studied. 2. The disaccharidase activities were located mainly in the small intestine and showed a non-uniform pattern of distribution along the small intestine; trehalase activity was highest in the proximal part, lactase and cellobiase activities were highest in the proximal and middle parts and maltase activity was highest in the distal part. 3. The intestinal lactase and cellobiase activities were highest in the young calf and decreased with age, whereas the intestinal maltase and trehalase activities, which were very low compared with the lactase activity, did not change with age. 4. No intestinal sucrase or palatinase activity was detected in the calf or in the adult cow. 5. Homogenates of intestinal mucosa also exhibited amylase and dextranase activity. 6. Homogenates of the pancreas possessed a strong amylase activity and a weak maltase activity. The maltase activity did not change with age, whereas the amylase activity increased with age. 7. No marked differences were observed between the carbohydrase activities of calves fed solely on milk and those of calves given a concentrate-hay diet from 6 weeks of age.
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PMID:Carbohydrase activities in the bovine digestive tract. 567 28

In the course of screening amylase inhibitor producing, microorganisms, a strain identified as Streptomyces nigrifaciens NTU-3314 was found to have the highest inhibitor-producing ability among the other isolated strains. This strain was aerobically cultured at 30 degrees C in a 5l jar fermentor with a working volume of 2l. The optimum cultural medium consisted of defatted soybean flake 3.0%, potato starch 4.0%, casein 0.6%, sucrose 0.6%, serine 0.02% and NaCl 0.8% (pH 7.0). With an aeration rate of 1.5 vvm, an agitation speed of 300 rpm and an inoculum of 15% seed (previously grown in seed medium 3), the highest amount of inhibitor was obtained after 24 hours of cultivation. The amylase inhibitor produced had inhibitory effects on both alpha-amylase and glucoamylase, but not on beta-amylase, alpha-glucosidase, beta-glucosidase or dextranase. It was quite stable in 0.1M phosphate buffer (pH 7.0) and nearly 100% of its activity was retained even after boiling at 100 degrees C for 20 min.
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PMID:The microbial production of amylase inhibitor and its application. I. Isolation and cultivation of Streptomyces nigrifaciens NTU-3314. 608 1

The activity of enzymes releasing glucose and reducing sugars from sucrose, maltose, starch and dextran was compared in the same pooled samples of plaque fluid (PF) from 24 h human dental plaque. Equimolar amounts of glucose and fructose were released from sucrose in 3 h incubations. Reducing activity was released from sucrose or starch at a similar rate. The rate of glucose release from the starch substrate was similar to that from maltose but lower than that from sucrose. Raffinose was hydrolysed, indicating beta-fructosidase activity in PF. The hydrolysis of maltose, trehalose and melezitose confirmed the presence of alpha-glucosidase activity. Maltose was metabolized partially to a maltosaccharide. No dextranase activity was detectable in PF, and the soluble polymeric carbohydrate in PF was partially degraded by fungal dextranase. Starch was degraded to dextrins, maltose and glucose.
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PMID:Hydrolysis of some carbohydrate substrates by enzymes of pooled human dental plaque fluid. 617 18

The action of certain substances known to induce cellular alterations, or encounted in the oral cavity, on the accumulation of 18F by Streptococcus mutans GS-5 has been investigated. A 62-67% inhibition in the number of 18F atoms bound per mg dry weight of cells could be induced by a 15 min pretreatment with 2.7 X 10(-4) M cetyltrimethylammoniumbromide, 1 X 10(-1) M acetic anhydride, or 7 X 10(-2) M HCl. Plate counts indicated that alteration of the cellular composition rather than viability was responsible for this diminution in 18F accumulation. Prior exposure for 15 min of this organism to 1 M HCHO or 0.1 M NaOH did not alter 18F accumulation. Of the common salts encountered in the oral cavity, CaCl2 enhanced 18F binding. Pretreatment of the assay cells for 15-160 min with 0.1-10 mg/ml of trypsin, pronase, protease, alpha-glucosidase, dextranase, or lactoferrin had no significant effect on the accumulation of 18F. However, pre-exposure of cells for 60 min to 1-10 mg/ml of either amylase or lipase induced a 40-67% inhibition in the binding of 18F, while lysozyme enhanced the binding of 18F by the cells. It would appear then that the binding of 18F by S. mutans may be altered by certain substances encountered in the oral cavity.
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PMID:The action of selected agents on the accumulation of 18F by Streptococcus mutans. 618 42

The thermophilic fungus Thermomyces lanuginosus, which is able to use dextran as primary carbon source for growth, excreted during the early phases of growth an enzyme activity capable of degrading dextran. The activity peaked at 22 h and decreased rapidly after the culture entered the stationary phase, probably caused by protease activity. Results from growth on a number of different carbon sources showed that polymer carbohydrates yielded the highest dextranase activities. On the basis of the substrate specificity and the release of glucose in the alpha-anomeric form from the hydrolysis of maltose, it is proposed that the enzyme responsible for the necessary degradation of dextran to smaller saccharides is an alpha-glucosidase.
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PMID:Extracellular alpha-Glucosidase with Dextran-Hydrolyzing Activity from the Thermophilic Fungus, Thermomyces lanuginosus 867 90

The enzymological studies on the sediment of the accumulation lake that has the main purpose of supplying drinking water to the city of Cluj-Napoca and the nearby villages, were aimed at the comprehensive understanding of the complex processes that happen in these habitats of special significance. In the sediment samples the following enzymatic activities have been quantitatively determined: phosphatase, actual and potential dehydrogenase, catalase, urease and protease. Non-enzymatic catalytic activity was also measured. Based on the relative values for the enzymatic activities, the enzymatic indicator of the sediment quality (EISQ) was calculated (ranging from 0.1 to 0.7). The enzymatic activities have been qualitatively determined for maltase, saccharase, lactase, cellobiase, amylase, dextranase, levanase, cellulase and inulinase. The correlation between the enzymatic and bacteriologic potential was statistically calculated.
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PMID:The enzymatic activity from the sediment of the Gilau dam reservoir - Cluj county. 1662 16