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)

In order to gain more insight into the adaptative mechanism of intestinal enzymes to dietary factors in rats, modifications in the activities of disaccharidases and aminopeptidase were measured after refeeding of a 70% solution of sucrose for 15 h following a 2-day fast. Mature epithelial cells from the villus and immature cells from the crypt were isolated after sequential removal of the cells along the villus-crypt axis. Synthesis of brush border disaccharidases was determined by measuring [3H]valine incorporation into proteins. 1. In the whole mucosa, a highly significant increase in sucrase and maltase activities and a significant drop in aminopeptidase activity was observed in the brush border membranes after sucrose refeeding. 2. Stimulation of sucrase and maltase activities in sucrose refed rats was produced mainly in the immature cells of the crypt and lower villus compartment. 3. After separation of the brush border proteins by SDS gel electrophoresis from villus and crypt cells of sucrose refed rats, major incorporation of the radioactive precursor occured in the protein bands corresponding to sucrase and maltase activities of the lower villus and crypt cell brush borders. These findings demonstrate that sucrase stimulation by sucrose occurs mainly in the immature epithelial cells and that the substrate induces de novo synthesis of sucrase molecules.
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PMID:Effect of sucrose refeeding on disaccharidase and aminopeptidase activities of intestinal villus and crypt cells in adult rats. Evidence for a sucrose-dependent induction of sucrase in the crypt cells. 677 Sep 8

Maltase from Saccharomyces cerevisiae-II was purified by ion-exchange chromatography on DEAE-Sephadex A-50 and isoelectric focusing. The purification procedure resulted in two enzyme isoforms with pI of 5.35 and 5.3 and identical specific activities. The molecular weights of the isoforms as determined by SDS polyacrylamide gel electrophoresis and gel filtration through Sephadex G-100 are 60 000 and 55 000, respectively. Both isoforms were electrophoretically polydisperse. The maltase isoforms are glycoproteins containing 1.5-2% of glucosamine and 5-8% (isoform A) and 2-3% (isoform B) of neutral sugars. Using paper chromatography and glucose oxidase, it was shown that glucose is an indispensable constituent of neutral sugars in both isoforms.
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PMID:[Isolation and properties of maltase from Saccharomyces cerevisiae-II]. 701 1

We studied the effect of intestinal microorganisms on the synthesis of membrane-associated glycoproteins in the upper small intestine by intraperitoneally administering L-[3H]fucose, D-[14C]glucosamine, or L-[3H]leucine to germ-free mice and mice exposed to microorganisms for 4 weeks (conventionalized). The incorporation of the labeled compounds into sucrase-isomaltase complex and maltase was determined by immunoprecipitating Triton X-100-solubilized microvillus membranes with their antibodies. Purified microvillus membranes from germ-free and conventionalized mice differed in the activities of some marker enzymes but not in the number and mobility of the components on SDS-polyacrylamide gel electrophoresis. Maximal incorporation of [3H]fucose and [14C]glucosamine into the microvillus membrane and two enzymes was reached 2-3 h post-injection in both groups, however, the amounts incorporated were larger in conventionalized mice. There was little difference in [3H]leucine incorporation into the total glycoproteins of microvillus membranes between the two groups. Our results suggest that the introduction of microorganisms stimulates the synthesis of sugar chains of microvillus membrane-associated glycoproteins. The enhanced in vitro fucosyltransferase activity in conventionalized mice partly supports this suggestion.
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PMID:Biosynthesis of microvillus membrane-associated glycoproteins of small intestinal epithelial cells in germ-free and conventionalized mice. 713 Jan 48

alpha-Glucosidase was partially purified 103-fold from a cell-free extract of Torulaspora pretoriensis YK-1 by column chromatography on Toyopearl HW55F, DEAE-Toyopearl 650M, hydroxylapatite and phenyl-Toyopearl 650M. Further purification by preparative polyacrylamide gel electrophoresis (PAGE) gave the homogenous protein, but the specific activity was reduced. The molecular weight of the enzyme was estimated to be 69,000 by SDS-PAGE and 60,000 by gel filtration. Optimum pH and temperature were 6.8 and 35 degrees C, respectively. The enzyme was inhibited strongly by AgNO3, HgCl2, sodium dodecyl sulfate, and N-ethylmaleimide. The Km (mM) for p-nitrophenyl alpha-D-glucopyranoside, maltose, maltotriose, isomaltose, methyl alpha-glucoside, and sucrose were 0.15, 150, 45, 17, 18, and 29, and Vmax (mumol/min/mg protein) for those substrates were 87, 0.23, 2.4, 9.0, 12, and 7.4, respectively. The N-terminal amino acid sequence of the enzyme was PEVKNHPETQPKWWKEATVY. The properties of alpha-glucosidase from T. pretoriensis YK-1 were similar to those from Saccharomyces cerevisiae.
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PMID:Purification and characterization of alpha-glucosidase from Torulaspora pretoriensis YK-1. 776 39

We tested the effect of dietary fat on the lipid composition and hydrolase activity of jejunal brush border membranes in piglets. Eighteen 5-wk-old piglets were divided into three groups and for 4 wk fed either an unsaturated low fat diet (3.2% corn oil), an unsaturated high fat diet (17.2% corn oil) or a saturated high fat diet (2.2% corn oil + 15% tallow). Brush border membranes were prepared from the jejunal mucosa and analyzed for cholesterol, phospholipid and fatty acids. The activities of sucrase-isomaltase, lactase-phlorizin hydrolase, maltase-glucoamylase, aminopeptidase and alkaline phosphatase were measured. Lactase-phlorizin hydrolase isoforms were immunopurified and separated by SDS-PAGE, and their relative proportions were measured by densitometry. The activities of the disaccharidases and alkaline phosphatase, but not aminopeptidase, were greater in animals fed the saturated high fat diet than in animals fed the unsaturated high fat diet. The fatty acid composition of the membranes generally reflected the composition of the diet. Correlation analysis demonstrated that the phospholipid, fatty acid and cholesterol compositions of the membranes were associated with the differences in brush border hydrolase activity.
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PMID:Jejunal brush border hydrolase activity is higher in tallow-fed pigs than in corn oil-fed pigs. 793 9

Pig brain cytosolic sialidase purified to homogeneity, showed a single protein band on SDS-PAGE under non-reducing conditions, and three bands using reducing conditions, suggesting a complex of different units. The sialidase complex (molecular mass, M(r), 180 kDa) was resolved into a catalytic unit (M(r) 30 kDa), active but very liable upon storage at 4 degrees C and freezing and thawing, and two protective units (66 kDa and 42 kDa), inactive, but capable to stabilize the catalytic unit. Recombination of the catalytic and protective units (optimal ratio, 1:1, by weight) gave rise to a stable active complex. Using GD1a as substrate, the catalytic unit showed a Michaelis-Menten kinetics, and the complex a sigmoid-shaped kinetics, whereas a Michaelis-Menten kinetics was exhibited with MU-NeuAc in both cases. The apparent Vmax and Km values of the catalytic unit for MU-NeuAc and GD1a were 105.1 and 110.0 mU/mg protein, and 4.2 x 10(-5) and 1.6 x 10(-5) M, respectively. The model we propose for cytosolic sialidase complex is one of each protective units and 2-3 catalytic units. The sialidase complex and protective units did not display any beta-D-galactosidase, beta-D-N- acetylglucosaminidase, alpha-L-fucosidase, alpha-D-glucosidase and carboxypeptidase activities.
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PMID:Cytosolic sialidase from pig brain: a 'protein complex' containing catalytic and protective units. 794 53

The inhibitory properties of bromoacetyl-p-aminohippuric acid as the affinity probe of the organic anion transport system were studied. Bromoacetylated p-aminohippurate was shown to be able to inhibit irreversibly the p-aminohippurate (PAH) uptake in brush-border membrane vesicles. The inhibition depends on both the time of treatment and the affinity probe concentration. The treatment of brush-border membrane with 1 mM bromoacetyl-p-aminohippurate for 1.5 h results in 100% irreversible inhibition of PAH transport but no changes were observed in the activity of alkaline phosphatase, gamma-glutamyltranspeptidase or maltase. The affinity labelling of the organic anion transporters was performed with bromoacetyl-p-amino[3H]hippuric acid. It was shown, by means of SDS-polyacrylamide gel electrophoresis, that the probe bound covalently to the brush-border membrane proteins with molecular masses of 28 kDa, 63 kDa, 98 kDa, and > 150 kDa. The data obtained with SITS and probenecid as the organic anion transport inhibitors indicate that brush-border membrane proteins of 28 kDa, 63 kDa, 98 kDa may correspond to the organic anion transport system.
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PMID:Affinity identification of organic anion transporters in brush-border membrane vesicles from rat kidney. 820 41

Two isoenzymes of maltase (EC 3.2.1.20) were purified to homogeneity from Candida albicans. Isoenzymes I and II were found to have apparent molecular masses of 63 and 66 kDa on SDS/PAGE with isoelectric points of 5.0 and 4.6 respectively. Both isoenzymes resembled each other in similar N-terminal sequence, specificity for the alpha(1-->4) glycosidic linkage and immune cross-reactivity on Western blots using a maltase II antigen-purified rabbit antibody. Maltase was induced by growth on sucrose whereas beta-fructofuranosidase activity could not be detected under similar conditions. Maltase I and II were shown to be unglycosylated enzymes by neutral sugar assay, and more than 90% of alpha-glucosidase activity was recoverable from spheroplasts. These data, in combination with other results from this laboratory [Geber, Williamson, Rex, Sweeney and Bennett (1992) J. Bacteriol. 174, 6992-6996] showing lack of a plausible leader sequence in genomic or mRNA transcripts, suggest an intracellular localization of the enzyme. To establish further the mechanism of sucrose assimilation by maltase, the existence of a sucrose-inducible H+/sucrose syn-transporter was demonstrated by (1) the kinetics of sucrose-induced [14C]sucrose uptake, (2) recovery of intact [14C]sucrose from ground cells by t.l.c. and (3) transport of 0.83 mol of H+/mol of [14C]sucrose. In total, the above is consistent with a mechanism whereby sucrose is transported into C. albicans to be hydrolysed by an intracellular maltase.
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PMID:Role of maltase in the utilization of sucrose by Candida albicans. 848 4

The enzymes responsible for much of the isomaltase and maltase activities in the intestine of the frog, Rana japonica, were purified by detergent solubilization and affinity chromatography on Sephadex G-200 gel. The two activities paralleled each other during purification. The isomaltase, maltase and glucoamylase activities eluted in the same pattern on Sepharose 4B gel filtration as well as on Sephadex G-200 gel affinity chromatography. Anti-rabbit sucrase-isomaltase antibody inhibited the isomaltase activity but not the maltase or glucoamylase activity of the purified enzyme preparation, while the three activities were precipitated in parallel by the antibody. The isomaltase activity was more stable at 55 degrees C than the maltase and glucoamylase activities. On SDS-polyacrylamide gel electrophoresis under nondissociating conditions the purified enzyme preparation showed only one major band of 330 kDa, while under dissociating conditions it showed two bands of 116 and 212 kDa. These results suggest that isomaltase (apparently with no or minor maltase activity) is due to a protein domain (or protein) different from one which is responsible for maltase and glucoamylase activities. This implies that isomaltase is associated with maltase/glucoamylase to form alpha-glucosidase complex in the brush border membrane of the frog intestine.
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PMID:Purification and characterization of alpha-glucosidase complex from the intestine of the frog, Rana japonica. 881 21

When Mucor javanicus was cultured with castanospermine, two alpha-glucosidases (CS-I, II) were produced. The two enzymes were purified by two CM-cellulofine column chromatographies, and compared with the alpha-glucosidase (C) from a culture without castanospermine. The molecular weights of the three enzymes were calculated to be 97,000 (CS-I, II) and 94,000 (C) from SDS-PAGE. CS-II was similar in hydrolysis of alpha-1,4-linkage to C, but hydrolyzed alpha-1,2-, alpha-1,3-, and alpha-1,6-linkages at a lower rate than C. The Michaelis constant of CS-I for malto-oligosaccharides was several times as high as the constants of CS-II and C, but CS-I hydrolyzed nigerose at a faster rate than maltose.
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PMID:Two forms of alpha-glucosidase from Mucor javanicus produced by culture with castanospermine. 890 Nov 14


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