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

The effects of bilateral adrenalectomy and subsequent force-feeding of L-tryptophan (30 mg/100 g body weight) on the activity of disaccharidases (lactase, sucrase, and maltase) in the jejunum and ileum were investigated. One month after adrenalectomy the activity of lactase, sucrase, and maltase in the ileum and of lactase and maltase in the jejunum was significantly decreased when compared with that of the sham-operated controls. In adrenalectomized rats, administration of tryptophan (24 h later) produced significant increments in lactase and maltase activities in both jejunum and ileum, compared with the corresponding water-fed adrenalectomized control.
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PMID:Effect of adrenalectomy and tryptophan force-feeding on the activity of intestinal disaccharidases in adult rats. 677 Apr 55

The contribution deals with histochemical localization of alpha-glucosidase, beta-glucosidase, beta-galactosidase and beta-glucuronidase in the mesencephalon of fresh water turtle. These enzymes demonstrate strong activity in all the myelinated fibers. Neuronal elements of nucleus ruber, nucleus isthmi, torus semicircularis, third and fourth cranial nerve nuclei, nucleus profundus mesencephali etc. demonstrate variable activity. Interestingly enough, there is parallel localization of all these enzymes in nuclei and tracts of mesencephalon. Further, the pattern of phospholipids and neutral lipids localization is almost identical to that of glycosidases. Since lipids and carbohydrates are rich source of energy in the central nervous system, and these enzymes are involved in their breakdown, their possible role in nerve cells and fibers of mesencephalon of turtle has been discussed.
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PMID:Significance of glycosidases in lipid and carbohydrate metabolism II. Studies in the mesencephalon of fresh water turtle (Lissemys punctata). 681 15

The previously isolated recessive mutant allele hex2-3 of Saccharomyces cerevisiae caused a defect in carbon catabolite repression of maltase, invertase, malate dehydrogenase, and respiration but at the same time led to an extreme sensitivity to maltose (Zimmerman and Scheel, 1977; Entian and Zimmermann, 1980). Addition of maltose to a growing culture of a hex2-3 mutant resulted within 60 to 90 min in an inhibition of growth, glycolysis, and de novo protein synthesis. This was not accompanied by any abnormal levels of glycolysis metabolites or glycolytic enzyme activities. However, inhibitory effects coincided with a dramatic increase in intracellular glucose up to 150 mM relative to cell water as opposed to 2.5 mM in wild-type cells. This abnormal behavior is interpreted as a result of an uncontrolled maltose uptake in hex2 mutants, which in combination with increasing maltase activity results in an accumulation of intracellular glucose. Obviously the amount of available glucose surpassed glycolytic capacity in hex2 mutants. Properties of mutant alleles hex2 and hex1 (see Entian and Zimmermann, 1980) clearly show, that specific gene functions are involved in adapting the rate of sugar uptake into the cell to the actual glycolytic capacity.
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PMID:A defect in carbon catabolite repression associated with uncontrollable and excessive maltose uptake. 700 23

We compared the absorption of carbohydrate from solutions of glucose oligomers and glucose in jejunal Thiry-Vella fistulae, a preparation deprived of pancreatic secretions. The studies were performed with two concentrations (90 and 360 mg/dl) of both glucose and the glucose oligomers. Carbohydrate absorption from glucose solutions (33.1 +/- 2.8, 115.9 +/- 8.9 micrograms/cm/min) was significantly greater (P less than 0.025; P less than 0.005) than that from oligomer solutions (26.6 +/- 2.1 and 92.4 +/- 9.0 micrograms/cm/min). Thin-layer analyses of the perfusates demonstrate digestion of oligomers with a chain length up to eleven and suggest digestion of oligomers of even greater chain length. Atrophy of the jejunal mucosa occurred over the course of the study as evidenced by a decrease in the ratio of villous height to crypt depth from 3.8 to 0.3, and by a 80% decrease in the activity of maltase, sucrase, and lactase. Atrophy was accompanied by a significant decline in the absorption of both glucose oligomers (P less than 0.005) and glucose (P less than 0.01) from the more concentrated solutions but the decrement in absorption of both carbohydrates was similar: glucose oligomers, 79.3 +/- 19.4 micrograms/cm/min; and glucose, 69.8 +/- 14 micrograms/cm/min (P greater than 0.20). Water absorption was enhanced by both carbohydrates, but there was no demonstrable difference between solutions of glucose and glucose oligomers. The osmolality of the solutions clearly influenced water absorption (P less than 0.025) but failed to effect the absorption of carbohydrates.
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PMID:The jejunal absorption of glucose oligomers in the absence of pancreatic enzymes. 722 Jan 47

Freshwater turtles Trachemys scripta elegans endure prolonged severe hypoxia, and even complete anoxia, while diving or hibernating underwater. Metabolic adaptations supporting survival include the activation of glycogenolysis and glucose output from liver, as well as strong metabolic rate depression. The present study analyzes the enzymes of both the phosphorolytic (glycogen phosphorylase, phosphorylase b kinase, cAMP-dependent protein kinase) and glucosidic (alpha-glucosidase) pathways of glycogenolysis in turtle organs. Turtles were subjected to 5 hr of submergence in N2-bubbled water at 7 degrees C and then activities of phosphorolytic and glucosidic enzymes were assayed in liver, heart, brain, and red and white skeletal muscle, and compared with aerobic controls. In vitro incubations also assessed protein kinase A control of phosphorolytic enzymes. A functional enzyme cascade system for the activation of glycogen phosphorylase was found in all organs, and both phosphorylase and phosphorylase kinase were stimulated by in vitro incubation with the catalytic subunit of cAMP-dependent protein kinase. Anoxic submergence led to significant increases in phosphorylase activities in liver and heart (phosphorylase a rose 2- and 2.5-fold, respectively) but phosphorylase kinase and protein kinase A activities in liver were reduced after 5 hr exposure. Both acidic (pH 4) and neutral (pH 7) forms of alpha-glucosidase were detected in all five organs with highest activities in liver. Activity of acid alpha-glucosidase, which degrades lysosomal glycogen, increased by 2-fold in liver during anoxic submergence. The data show that glycogen breakdown in turtle liver during anoxic submergence may result from coordinated activations of both the cytoplasmic phosphorolytic and the lysosomal glucosidic pathways of glycogenolysis.
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PMID:Enzymatic control of glycogenolysis during anoxic submergence in the freshwater turtle Trachemys scripta. 758 17

Three castrated male Holstein cattle (423 (SD 19)kg live weight) fitted with elevated carotid artery, portal, and mesenteric venous catheters, and abomasal and ileal cannulas were used to study small-intestinal starch digestion. The cattle were infused abomasally with water (275 ml/h), glucose (66 g/h), maize dextrin (66 g/h) or maize starch (66 g/h) in an incomplete Latin square design, with eight infusion periods. Infusion with carbohydrate resulted in higher arterial glucose concentrations and greater net portal glucose flux than when cattle were infused with water. Arterial glucose concentration and net portal glucose flux were highest when glucose was infused. In the small intestine, 85% of abomasally-infused glucose, 78% of infused dextrin, and 66% of infused starch disappeared. Of the carbohydrate that disappeared in the small intestine, that which could be accounted for as net portal glucose flux was 73% for glucose, 60% for dextrin, and 57% for starch. Ileal digesta contained unpolymerized glucose, and short-chain soluble alpha-glucoside. Of the infused dextrin flowing past the ileum (14 g/h), 0.3 g/h was glucose, 6.2 g/h was soluble alpha-glucoside, and 7.5 g/h was insoluble alpha-glucoside. Of the infused starch flowing at the ileum (22.2 g/h), 0.9 g/h was glucose, 5.3 g/h was soluble alpha-glucoside, and 15.9 g/h was insoluble alpha-glucoside. The average chain lengths of the soluble alpha-glucosides in ileal digesta were 2.07 and 2.36 for dextrin and starch infusions respectively, indicating mostly di- and to a lesser extent trisaccharides. We conclude that (1) when 66 g raw starch is presented to the small intestine per h, about half of the intestinal disappearance appears as glucose in the portal vasculature, and (2) alpha-1,4 glucosidase (EC 3.2.1.20) activity at the brush border is the rate-limiting step to small-intestinal starch digestion in cattle.
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PMID:Abomasal glucose, maize starch and maize dextrin infusions in cattle: small-intestinal disappearance, net portal glucose flux and ileal oligosaccharide flow. 762 94

Important variations in intestinal biochemical characteristics were recorded after ingestion of a single dose of spermine (8 mumol 50 microliters-1 water) by rats which were 11 days old. Two phases of events were observed. During the first hours which follow spermine administration, we mainly noted: -a decrease in the weight of DNA and of intestine per cm, -a decrease in the specific activity of lactase and of maltase, -an increase in the spermine content. The second phase of events started about 30 h after spermine ingestion. We observed: 1. An increase in the weight of DNA and of intestine per cm; 2. The appearance of sucrase activity; 3. An increase in maltase specific activity; 4. An increase in spermidine content; 5. tendency to normalization of the spermine content. The epithelial cells of the proximal intestine were isolated in fractions from the top of the villi to the bottom of the crypts. Two hours after spermine administration, we noted: 1. An increase in the lactase specific activity of the epithelial cells located at the top of the vili; 2. A decrease in the activity of the cells situated at the lower part of the crypts; 3. An increase in the specific activity of maltase contained in the different categories of enterocytes, except in those from the bottom of the crypts; 4. An increase in the content of putrescine present in the epithelial cells of the whole axis excepted in the bottom of the crypts; 5. An increase in the spermidine and spermine content of all the cell fractions.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Evolution of biochemical parameters characterizing the proximal small intestine after orally administered spermine in unweaned rats. 806 97

We investigated the effect of polydextrose, one of the water-soluble non-digestible polysaccharides, on the activities of brush-border membrane enzymes of small intestine in rats and on glucose absorption with relation to the thickness of the unstirred water layer in humans. Rats were fed a 5% polydextrose-supplemented elemental diet for 2 or 4 wk. The mucosal alkaline phosphatase, maltase, and sucrase activities were measured in the upper, middle, and lower intestine. There was no significant difference between control and polydextrose groups. The potentiometric tube was inserted orally in the jejunum. Glucose absorption was measured by perfusion with the solutions with or without 5% polydextrose. There was no significant difference in the glucose absorption rate or the thickness of the unstirred water layer between control and polydextrose solutions. The increase in viscosity of the polydextrose solution was negligible. This study indicated that polydextrose had no effect on the thickness of the unstirred water layer and did not inhibit glucose absorption in humans.
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PMID:Polydextrose and activities of brush-border membrane enzymes of small intestine in rats and glucose absorption in humans. 835 63

Oolong tea extract (OTE) was found to inhibit the water-insoluble glucan-synthesizing enzyme, glucosyltransferase I (GTase-I), of Streptococcus sobrinus 6715. The GTase-inhibitory substance in the OTE was purified successive adsorption chromatography on Diaion HP-21 and HP-20 columns; this was followed by further purification by Sephadex LH-20 column chromatography. A major fraction that inhibited GTase activity (fraction OTF10) was obtained, and the chemical analysis of OTF10 indicated that it was a novel polymeric polyphenol compound that had a molecular weight of approximately 2,000 and differed from other tea polyphenols. Catechins and all other low-molecular-weight polyphenols except theaflavin derived from balck tea did not show significant GTase-inhibitory activities. It was found that OTE amd PTF10 markedly inhibit GTase-I and yeast alpha-glucosidase, but not salivary alpha-amylase. Various GTases purified from S. sobrinus and Streptococcus mutans were examined for inhibition by OTE and OTF10. It was determined that S. sobrinus GTase-I and S. mutans cell-free GTase synthesizing water-soluble glucan were most susceptible to the inhibitory action of OTF10, while S. sobrinus GTase-Sa and S. mutans cell-associated GTase were moderately inhibited; no inhibition of S. sobrinus GTase-Sb was observed. Inhibition of a specific GTase or specific GTases of mutants streptococci resulted in decreased adherence of the growing cells of these organisms. The inhibitory effect of OTF10 on cellular adherence was significantly stronger than that of OTE.
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PMID:Inhibitory effect of oolong tea polyphenols on glycosyltransferases of mutans Streptococci. 848 34

A novel derivative of vitamin E, vitamin E glucoside, was synthesized from 2-hydroxymethyl-2,5,7,8-tetramethylchroman-6-ol and maltose in a solution containing DMSO by transglycosylation with alpha-glucosidase from Saccharomyces species. The glycosylated product was identified as 2-(alpha-D-glucopyranosyl)methyl-2,5,7,8-tetramethylchroman-6-ol (TMG) by mass spectrometry and nuclear magnetic resonance spectroscopy. The optimal pH of transglycosylation was 5.5, and the yield of TMG increased as the concentration of maltose increased. TMG has high solubility in water (> 1 x 10(3) mg/mL). The 1,1-diphenyl-2-picrylhydrazyl radical scavenging activity of TMG was found to be nearly the same as those of alpha-tocopherol, Trolox (2-carboxy-2,5,7,8-tetramethylchroman-6-ol), and ascorbic acid.
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PMID:Synthesis of a novel vitamin E derivative, 2-(alpha-D-glucopyranosyl) methyl-2,5,7,8-tetramethylchroman-6-ol, by alpha-glucosidase-catalyzed transglycosylation. 907 96


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