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)

Purified sucrase-isomaltase complex sucrose alpha-glucohydrolase, EC 3.2.1.48 - dextrin 6-alpha-glycanohydrolase, EC 3.2.1.10) solubilized by papain from rabbit intestine was dissociated by citraconylation into its subunits, sucrase and isomaltase, which were then isolated in a form active immunologically as well as enzymatically by affinity chromatography on Sephadex G-200 and gel-filtration on Bio-gel P-300. Antibodies against the purified complex inhibited isomaltase but not sucrase and formed precipitation lines, crossing each other, with isolated sucrase and isomaltase, showing that the two enzymes differ in antigenicity from each other. By absorbing the antibodies with isolated sucrase and isomaltase, antibodies specific for isomaltase and sucrase, respectively, were obtained. Like the original antibodies, both of the specific antibodies quantitatively agglutinated microvillous vesicles. Sucrase was inhibited by neither of the antibodies. In contrast, isomaltase was greatly inhibited by the isomaltase-specific antibodies, but not by the sucrase-specific ones.
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PMID:Immunochemical studies on the subunits of rabbit-intestinal sucrase-isomaltase complex. 7 Feb 24

Mcrovilli membranes have been isolated from dog jejunal and ileal enterocytes. Proteins were analysed by polyacrylamide gel electrophoresis after solubilization with sodium dodecylsulphate. The recovery of the membrane fraction with this purification method was found to be 22% and the specific activity of sucrase increases 19 folds in the membrane fraction. Microvilli membrane proteins after polyacrylamide gel electrophoresis were seprated in 21 bands, most of them with a molecular weight higher than 70 000. Seven bands with molecular weight from 150 000 to more than 340 000, were found to be glycoproteins.
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PMID:[Microvilli membrane proteins from dog enterocytes]. 7 Oct 83

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

The intestinal dipeptidase and disaccharidase activities were investigated in 120 male albino rats of the Wistar strain after administration of 21 mumol.kg-1 body weight phosalone, 14.8 mumol.kg-1 body weight lindane and 10.5 mumol.kg-1 body weight phosalone combined with 7.4 mumol.kg-1 body weight lindane. The dipeptidase activity under the effect of these comparatively low doses of pesticides reveals slightly to moderate changes. The activity of intestinal disaccharidases after a 90-day phosalone and lindane treatment is markedly decreased, particularly that of sucrase. The mechanism of these changes remains unknown.
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PMID:Effect of the pesticides phosalone and lindane on the activity of some dipeptidases and disaccharidases in rat intestinal mucosa. 9 5

The activity of pectine-lyase, polygalacturonase, pectine-methyl-esterase, amylase, and saccharase in Pythium ultimum, Pythium oligandrum, and Pythium debaryanum was determined. Cultures of fungi were cultivated under different temperatures and pH-values within 24 hours and 15 days. The optimum temperature for production of the mentioned enzymes was found to be 24 degrees C. Furthermore, the influence of pH and age of culture on activity of enzyme was investigated. The same trend was found in all the fungus species examined.
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PMID:Activity of pectinases, amylases, and saccharase in Pythium spp. 9 72

The use of a commercial oscillating-tube densitometer with an accuracy of 4 . 10(-7) g/cm3 for the determination of enzyme-kinetics constants is tested. This method is applied to the investigation of the influence of vitamin C (sodium ascorbate) on the glycolytic enzymes invertase, dextransucrase and dextranase. Invertase is inhibited uncompetitively, dextransucrase non-competitively. There is no significant effect of the vitamin on dextranase. The comparison of the mechanisms of the three enzymes suggests that only those reaction steps are inhibited by vitamin C in which fructose is released from the enzyme.
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PMID:The use of an oscillating-tube densitometer as a tool in enzyme kinetics. Determination of the influence of sodium ascorbate on invertase, dextransucrase and dextranase. 9 45

A considerable increase occurs in D-glucose uptake and brush border sucrase and lactase activities in the intestine of monkeys treated with a single oral dose of DDT. Brush border alkaline phosphatase activity remains unaffected in the pesticide treated animals. In vitro addiction of DDT has no effect on the sugar absorption and disaccharidase activities.
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PMID:Effects of DDT (chlorophenotane) administration on glucose uptake and brush border enzymes in monkey intestine. 9 80

Extracellular caseinolytic activity was found in the culture fluid of Streptococcus sanguis ATCC 10556 grown in a dialyzed culture medium. This activity was due to multiple proteases that differed in their elution from hydroxyapatite, sensitivity to enzyme inhibitors, specificity and optimum pH. IgA protease, which splits human immunoglobulin A1 into intact Fc and Fab could be effectively separated from these relatively non-specific proteases and purified to apparent homogeneity in 20% yield by a five-step procedure. Although the bulk of the dextran sucrase activity was separated from the IgA protease, a small amount of sucrase activity remained with the final IgA protease preparation. In polyacrylamide gel electrophoresis at pH 9.5 both activities were located in the single protein band detected in this preparation. A quantitative method for the assay of IgA protease was developed, based on radial immunodiffusion to quantitate the Fab produced. This was used to follow the specific activity and yield during purification, and to characterize some of the catalytic properties of the enzyme. At an enzyme/substrate ratio of 1: 400 (w/w) the protease could effect 50% proteolysis of IgA in overnight incubation at 37 degrees C. The optimum activity was at pH 8.0, and 50% inhibition was achieved at 4 . 10(-4) M o-phenanthroline or 8 . 10(-4) M ethylene diamine tetraacetate. Concentrations of diisopropyl phosphofluoridate, phenylmethyl-sulfonyl fluoride, iodoacetate and p-chloromercuribenzoate up to 10(-2) M were without effect on the IgA protease activity. Full reactivation of the chelator inhibited enzyme could be achieved by the addition of Mg2+, Mn2+ or Ca2+.
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PMID:Studies on extracellular proteases of Streptococcus sanguis. Purification and characterization of a human IgA1 specific protease. 10 57

A sensitive protein-binding assay has been used to measure plasma concentrations of total corticosterone during postnatal development in the rat. These concentrations were extremely low on days 6--12, showed a significant rise by day 14, and then continued to rise until peaking on day 24. Plasma titers of corticosteroid-binding globulin rose even more dramatically from day 12 onward. Consequently, the percentage of total plasma corticosterone, which was protein-bound, showed a gradual rise from 78% on day 12 to 98% on day 24. Despite this trend, when concentrations of free corticosterone were calculated, they were found to have a developmental profile very similar to that of total corticosterone. Assay of jejunal lactase and sucrase in the same animals that were used for the corticosterone studies showed that the ontogenic rise of both total and free corticosterone preceded the developmental changes in the activities of these enzymes by approximately 2 days. The data suggest that the rise in free corticosterone that begins on day 14 acts as a cue for enzymic changes in both liver and intestine.
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PMID:Plasma concentrations of total and free corticosterone during development in the rat. 10 38

Starvation overnight and starvation for 48 h reduced the weight and the protein content of mucosal scrapings, but only minimally reduced the DNA content of the mucosal scrapings. The activity of sucrase and maltase was reduced by both periods of starvation. The activity of lactase and of acid and alkaline phosphatase, however, was less subject to starvation. There were striking differences in the response to starvation between the proximal, mid and distal third of the small intestine. The importance of the proper reference system was discussed.
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PMID:Effect of starvation on small intestinal enzyme activity in germ-free rats. 10 66


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