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

---

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

The effects of polysaccharides and tannins present in the hulls of field beans (Vicia faba L.) on the digestion of amino acids, starch and lipid were studied in poultry. A control diet without hulls and the same diet substituted with 400 g hulls/kg diet from three different varieties of beans were fed to 3-week-old chicks for 4 d. Digestibility coefficients for amino acids, starch and lipid were calculated from measurements made of these nutrients in the diets and the freeze-dried excreta with the aid of titanium dioxide as a marker. Activities of trypsin (EC 3.4.21.4), alpha-amylase (EC 3.2.1.1), and lipase (EC 3.1.1.3) in digesta removed from the upper jejunum, sucrase (EC 3.2.1.48) in the gut mucosa from the upper jejunum, and alpha-amylase and lipase in the pancreas were measured. The hulls were analysed for their polysaccharide and tannin contents. Results showed that the hulls were mostly carbohydrate in composition, with cellulose the predominant polysaccharide. Tannins present in the hulls of two coloured-flowering varieties (Brunette and Minica) were of the condensed type. The diet with tannin-free hulls (white-flowering variety Medes) lowered slightly the digestion of amino acids, starch and lipid compared with the control diet. This effect was believed to be due to inhibition of digestive enzymes, possibly through their adsorption onto the hulls. Diets with tannin-rich hulls (varieties Brunette and Minica) caused a large reduction in the digestion of amino acids, starch and lipid compared with the control diet mainly due to inactivation of digestive enzymes by the formation of tannin-enzyme complexes in the digestive tract. Enzyme activities could be partially restored by the addition of polyvinylpyrrolidone to the digesta. Tannins inactivated trypsin the most, alpha-amylase to a lesser extent and lipase the least and as a consequence lowered the digestion of amino acids the most, starch to a lesser extent and lipid the least. Tannins did not induce an increased pancreatic production of digestive enzymes, nor did they affect activity of jejunum mucosal sucrase. Condensed tannins from Brunette and Minica hulls were partially extractable in methanol alone, but required acidic methanol for fuller extraction. The vanillin:anthocyanidin ratio suggested that tannins were polymerized to the same degree in the Brunette and Minica varieties, both in the methanol and acidic methanol extracts. Hulls from the variety Minica contained a greater amount of methanol-extractable tannins, the quantity of remaining tannins that required acidic methanol for extraction being the same for both varieties.
...
PMID:The inhibitory effects of hull polysaccharides and tannins of field beans (Vicia faba L.) on the digestion of amino acids, starch and lipid and on digestive enzyme activities in young chicks. 164 91

The methylotrophic yeast Hansenula polymorpha, a host organism for the production of heterologous proteins, has been applied to produce the alpha-galactosidase from the plant Cyamopsis tetragonoloba (guar). The yeast/Escherichia coli shuttle expression vector used is based on the origin of replication of the endogenous 2 microns plasmid of Saccharomyces cerevisiae and the LEU2 gene of S. cerevisiae for selection in H. polymorpha. In the expression vector, the alpha-galactosidase is controlled by the methanol-regulated promoter from the methanol oxidase gene, MOX, of H. polymorpha. The signal sequence of SUC2 (invertase) from the yeast S. cerevisiae, was used to ensure secretion of the alpha-galactosidase enzyme. After transformation and stabilization, the expression vector was stably integrated in the genome. The active alpha-galactosidase enzyme was efficiently secreted (greater than 85%) and after methanol induction, the expression level was 42 mg/l. Amino-terminal sequencing of the purified alpha-galactosidase enzyme synthesized by H. polymorpha showed that the S. cerevisiae invertase signal sequence was correctly processed by H. polymorpha. The secreted alpha-galactosidase was glycosylated and had a sugar content of 9.5%. The specific activity of the alpha-galactosidase produced by H. polymorpha was 38 U mg-1 compared to 100 U mg-1 for the guar alpha-galactosidase. Deglycosylation of the H. polymorpha alpha-galactosidase restored the specific activity completely.
...
PMID:Expression of the alpha-galactosidase from Cyamopsis tetragonoloba (guar) by Hansenula polymorpha. 165 81

Lentiginosine, a dihydroxyindolizidine alkaloid, was extracted from the leaves of Astragalus lentiginosus with hot methanol and was purified to homogeneity by ion-exchange, thin-layer, and radial chromatography. A second dihydroxyindolizidine, the 2-epimer of lentiginosine, was also purified to apparent homogeneity from these extracts. Gas chromatography of the two isomers (as the TMS derivatives) showed that they were better than 95% pure; lentiginosine eluted at 8.65 min and the 2-epimer at 9.00 min. Both compounds had a molecular ion in their mass spectra of 157, and the NMR spectra demonstrated that both were dihydroxyindolizidines differing in the configuration of the hydroxyl group at carbon 2. Lentiginosine was found to be a reasonably good inhibitor of the fungal alpha-glucosidase, amyloglucosidase (Ki = 1 x 10(-5) M), but it did not inhibit other alpha-glucosidases (i.e., sucrase, maltase, yeast alpha-glucosidase, glucosidase I) nor any other glycosidases. The 2-epimer had no activity against any of the glycosidases tested.
...
PMID:Lentiginosine, a dihydroxyindolizidine alkaloid that inhibits amyloglucosidase. 233 69

Binding sites for horseradish peroxidase (HRP), with unusual properties, were detected on the surface of cultured and isolated cells after the cells (on cover slips) had been quickly dried, fixed in cold methanol, and post-fixed in a paraformaldehyde solution. The reaction for surface-bound HRP was suppressed by micromolar concentrations of glycoproteins such as invertase, equine luteinizing hormone (eLH) or human chorionic gonadotropin (hCG). The reaction was also suppressed by 20 mM CDP, UDP, GTP, NAD, and ribose 5-phosphate. Two to six times higher concentrations of GMP, fructose 1-phosphate, galactose 6-phosphate, mannose 6-phosphate, fructose 6-phosphate, and glucose 6-phosphate were required to suppress the binding reaction. AMP, ATP, heparin, mannan, and eight non-phosphorylated sugars showed relatively low competing potencies but fucoidin and alpha-lactalbumin were strong inhibitors. No addition of Ca2+ was required for the binding of HRP to the cell surface. However, calcium-depleted, inactive HRP did not compete with the binding of native (calcium-containing) HRP whereas H2O2-inactivated HRP suppressed the binding. GTP, NAD, ribose 5-phosphate, and EGTA accelerated the release of previously-bound HRP from the cell surface whereas glycoproteins (invertase, eLH, and hCG) did not do so. Addition of Ca2+ to GTP, NAD, ribose 5-phosphate or to EGTA prevented the accelerated release of HRP from the cell surface. It is suggested that calcium, present either in the surface membrane or in HRP itself, is involved in the binding of HRP to the cell surface and in the inhibition of binding by GTP, NAD, and ribose 5-phosphate. It is also suggested that alpha-lactalbumin, GTP, UDP, and CDP compete with the binding of HRP to a glycosyltransferase on the cell surface.
...
PMID:Unusual binding sites for horseradish peroxidase on the surface of cultured and isolated mammalian cells. Suppression of binding by certain nucleotides and glycoproteins, and a role for calcium. 309 11

The aim of our work is to show the importance of the role of hydrophobic bonds in maintaining Mg2+-ATPase or sucrase activity and Na+-coupled D-glucose uptake normal for the brush border of rat enterocytes. The activity of the two enzymes and the D-glucose uptake were therefore measured under the action of n-aliphatic alcohols and related to the fluidity determined by ESR. Three concentrations were used for the first eight alcohols, those of octanol being about 1500-times lower than those of methanol. For each alcohol the D-glucose uptake and the fluidity were linear functions of the logarithm of the concentration, the linear regressions being practically parallel and equidistant. The concentrations (C) of the eight alcohols inhibiting the D-glucose uptake by 80% were similar to those increasing the membrane fluidity by 3%. The linear relationship which existed in both cases between log 1/C and log P, P being octanol/water partition coefficients of the alcohols, was evidence of great sensitivity to the hydrophobic effect of the alcohols. Only the first alcohols, however, produced any notable inhibition of Mg2+-ATPase and sucrase. Hydrophobic bonds are thus shown to have little influence in maintaining the activity of Mg2+-ATPase and sucrase, but they modulate the Na+-coupled D-glucose uptake.
...
PMID:Sensitivity of Na+-coupled D-glucose uptake, Mg2+-ATPase and sucrase to perturbations of the fluidity of brush-border membrane vesicles induced by n-aliphatic alcohols. 614 7

Saccharomyces cerevisiae and the methylotrophic yeast Hansenula polymorpha have been used to express both full-length and a large hydrophilic domain of human thyroid peroxidase (TPO). Expression of TPO in S. cerevisiae, using the natural signal sequence or the yeast alpha-mating factor (MF alpha) signal sequence, resulted in undetectable or very low levels of recombinant TPO production. However, TPO was expressed when the natural TPO leader sequence was replaced by the yeast STE2 signal sequence. This recombinant TPO reacted with both rabbit anti-human TPO polyclonal and mouse anti-human TPO monoclonal antibodies on Western blots. In the case of H. polymorpha, TPO expression was achieved when the natural TPO leader sequence was replaced by the MF alpha leader and the construct placed under the control of the methanol-regulated promoter from the methanol oxidase gene. The recombinant TPO produced in H. polymorpha reacted with both TPO polyclonal and TPO monoclonal antibodies. No TPO was produced when the signal sequence of SUC2 (invertase) or the TPO natural signal sequence was used to direct expression.
...
PMID:Expression of human thyroid peroxidase in the yeasts Saccharomyces cerevisiae and Hansenula polymorpha. 837 16

Enzyme synthesis of methyl fructoside was studied using beta-fructofuranosidase from Sacharomyces cerevisiae and sucrose and methanol as substrates. Taking into account the inhibition and deactivation effects of methanol on the enzyme, a system with 4.9M (20%, v/v) methanol was selected. At this alcohol level, 35% of sucrose is converted to fructoside at low or high substrate concentrations. The effect of enzyme concentration, pH, and temperature on both the synthesis and the hydrolysis of the fructoside was investigated. It was found that if the reaction proceeds at pH 6.0, 4 degree C and/or 0.014 mg/mL (3 U/mL) of beta-fructofuranosidase at varying sucrose concentrations, methyl fructoside may be obtained with a minimum loss of the fructoside at the end of the reaction.
...
PMID:Selectivity of methyl-fructoside synthesis with beta-fructofuranosidase. 867 85

A major difficulty with isolating enzymatically or chemically released oligosaccharides from large-scale glycoprotein deglycosylation reactions is the time-consuming chromatography, desalting, and concentration steps required to prepare a glycan fraction of manageable proportions. To overcome these time and preparative chromatography equipment requirements, we have developed a rapid organic solvent precipitation/extraction procedure that allows sequential isolation of endo-beta-N-acetylglucosaminidase H (EC 3.2.1.96)-released high-mannose and hybrid, peptide-N(4)-(N-acetyl-beta-glucosaminyl) Asn amidase (EC 3.5.1. 52)-released complex, and beta-eliminated O-linked glycans without the need for intermediate chromatography, desalting, or concentration steps. The method involves precipitation of protein and released glycans at -20 degrees C in 80% acetone and extraction of the glycans from the pellet with 60% aqueous methanol after each deglycosylation step. Three pools of essentially salt- and detergent-free oligosaccharides (high-mannose/hybrid, complex, and O-linked) can be isolated in a high yield in 4 days with this protocol, which has been extensively tested using bovine RNase B, human bile salt-stimulated lipase expressed in Pichia pastoris, hen ovalbumin, bovine fetuin, bovine thyroglobulin, and several invertase preparations from wild-type and mutant yeast strains.
...
PMID:Selective organic precipitation/extraction of released N-glycans following large-scale enzymatic deglycosylation of glycoproteins. 1066 Apr 52

Hexagalloylglucose (3-O-digalloyl-1,2,4,6-tetra-O-galloyl-beta-D- glucose), which was isolated from the methanol extract of the galls of Quercus infectoria, significantly inhibited alpha-glycosidases such as sucrase, maltase and isomaltase. Its inhibitory activity was comparable to acarbose being used as a hypoglycemic agent, while the inhibitory activity on alpha-amylase was approximately 10 times lower than that of acarbose. The results indicate that, when compared to acarbose, hexagalloylglucose might reduce the side effects by reducing inhibition of alpha-amylase.
...
PMID:alpha-Glycosidase inhibitory activity of hexagalloylglucose from the galls of Quercus infectoria. 1082 Oct 56

The influence of four pesticides, e.g. glyphosate, paraquat, atrazine, and carbaryl, on the activities of invertase, urease and phosphatase of twenty-two soils, numbered as 1-22, was investigated. Soils displayed a general variability of enzyme activities with invertase being more abundant than urease and phosphatase in the order listed. The addition of glyphosate and paraquat activated invertase and urease activities in several soils. Increments of invertase activity ranged from a very low increase (+4%) up to +204% in soils 11 and 14, respectively. Smaller increases were measured for urease. A general inhibitory effect (from 5% to 98%) was observed for phosphatase in the presence of glyphosate. The effects of atrazine and carbaryl on the three soil enzymes were evaluated against that exhibited by methanol, the solvent used for their solubilization. In almost all soils, atrazine further inhibited invertase activity with respect to the inhibitory effect shown by methanol. By contrast, consistent activation effects (from 61% to 10217%) were measured for urease with methanol alone and/or methanol-pesticide mixtures. Contradictory results were observed with phosphatase. Similarities found between the results obtained with enzymes in soils and those measured with synthetic enzyme complexes (e.g. free enzymes and/or clay-, organo-, and organo-clay-enzyme complexes) exposed to the same pesticides allowed some relationships between responses of soil enzymes to pesticides and soil properties to be hypothesized.
...
PMID:Pesticide influence on soil enzymatic activities. 1168 Jul 37


1 2 Next >>

---