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)

This study was undertaken to investigate the effect of alcohol on the activity of jejunal disaccharidases (DS). The activity of DS in a preparation of purified brush border membrane of hamster jejunum was measured in the absence and in the presence (0.8 to 6.4% wt/vol) of ethanol. To compare the effect of alcohol on DS with its action on a brush border enzyme of a different group, we also measured the activity of alkaline phosphatase (AP) under similar conditions. Ethanol depressed the activity of sucrase, maltase, and lactase in a dose-dependent and time-dependent manner, but it stimulated the activity of AP. The ethanol-induced inhibition of DS was completely reversible. Kinetic studies indicate that ethanol depressed the Vmax and increased the Km of sucrase and lactase. The Vmax of maltase also decreased, but the Km of this hydrolase was not affected by ethanol. From the results of this study it would appear that acute exposure of the jejunal brush border to ethanol depresses the DS activity of the membrane and that (because the AP was not depressed) the ethanol-induced inhibition of DS is not the result of a general inhibition of all enzymes of the brush border.
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PMID:Effect of ethanol on disaccharidases of hamster jejunal brush border membrane. 11 61

Streptococcus mutans has been shown to produce extracellular invertase, dextransucrase, and levansucrase. The purpose of this work was to study the relative quantities of these enzymes in pure culture supernatant, and in samples from commonly used purification methods. The strain "Ingbritt" was selected because it is a well-defined human strain, available, and with well-known growth requirements. The samples were incubated with sucrose for the determination of free monohexoses, and the polysaccharide from ethanol precipitation was hydrolyzed as previously described. In cell supernatant the inversion effect exerted 75% of total sucrolytic power, the dextransucrase 20% and the levansucrase 5%. No method, tested in this work, could separate all the activities completely.
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PMID:Combined extracellular sucrolytic enzyme power from a strain of Streptococcus mutans, and purification results. 28 69

The effect of graded (5, 10, 20, and 50%) chronic ethanol administration on the intestinal brush border enzymic activities has been investigated in the rat at three levels of the intestinal tract (duodenum, jejunum, ileum). Ethanol has been administered for 8, 15, 30, and 90 days. A 30% to 50% decrease of sucrase and alkaline phosphatase results, showing that the effect of alcohol appears in the first 8 days of intoxication is not reversible after 8 days of an alcohol-free diet. The effect of ethanol is not limited to disaccharidases. Impairment of alkaline phosphatase, peptidases and also enterokinases is observed. The decrease is more marked in the duodenum and jujunum than the ileum. The decrease of enzymic activity is generally maximal after 30 days of intoxication. There is then little further deterioration or even significant improvement. At the 30th day of ethanol administration, a clearcut dose-response relationship has been established. The results obtained suggest that ethanol exerts an effect on the intestinal mucosa which is not directly correlated to morphological villus changes.
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PMID:Intestinal brush border enzymes and chronic alcohol ingestion. 57 90

Membranous hydrolysis of saccharose (membranous digestion) and synthesis of invertase in the intestinal epithelial cells of rats and mice following introduction of pharmacological agents were studied. Ethyl alcohol, luminal and atropine lowered both the invertased activity in the area of membranous digestion and the synthesis of the enzyime. Hexonium and pilocarpine also lowered the level of membranous hydrolysis, but not the formation of enzymes. Epinephrine and octadine, on the contrary, enhanced the intensity of both these processes. The disclosed pharmacological effects are considered in the light of features specific for the structural organization of enzymes in the area of membranous digestion.
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PMID:[Effect of pharmacological agents on the membrane hydrolysis of saccharose]. 65 82

Absorption of 57Co-labelled vitamin B12 - intrinsic factor (IF) complex and its binding to mucosal precipitate and brush border fractions of rat small intestine was studied in rats pair-fed with a liquid diet containing ethanol 5 g/100 ml, 35% of calories, or isocalorically substituted sucrose. IF was obtained from rats fasted for 18 h. and for each experiment the amount of vitamin B12 added was the minimum required to achieve maximum binding to IF. Rats fed alcohol exhibited hepatic steatosis, proliferation of smooth endoplasmic reticulum, and disordered mitochondria after 6 weeks on the diet, and absorption of vitamin B12, fed with IF by stomach tube, was reduced signficantly. In contrast, binding of 57Co-labelled vitamin B12 -IF complex to mucosal precipitate and brush border fractions was never less than that of fractions from control rats at 4, 8 and 12 weeks on the alcohol diet. Furthermore, binding to the brush border was significantly greater in alcohol-fed rats at 12 weeks whether expressed per unit of beta-naphthylamidase (EC 3.4.1.1) activity or per milligram of protein. Total mucosal sucrase (EC 5.2.1.26) and beta-naphthylamidase were unchanged or slightly increased (beta-naphthylamidase at 12 weeks) on the alcohol-containing diet indicating that total brush border membrane was not reduced. Total brush border binding activity was the same in alcohol-fed and control rats at each time period. These results indicate that malabsorption of vitamin B12 in rats fed alcohol cannot be due to decreased binding of the vitamin B12 - IF complex by brush border membrane receptors, or secondary to a net decrease in membrane receptors.
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PMID:Lack of effect of alcohol on small intestinal binding of the vitamin B12 - intrinsic factor complex. 97 75

The acute effects of intraduodenal administration of ethanol, 5 g/kg body weight, on intestinal activities of lipid-reesterifying and disaccharidase enzymes of the small bowel were studied. Results were compared to those produced in controls receiving isocaloric amounts of glucose by the same route. Acyl-CoA:monoglyceride acyltransferase, acyl-CoA synthetase (acid:CoA ligase (AMP) EC 6.2.1.3), sucrase, and lactase assays were performed on jejunal samples; acyl-CoA synthetase assay was performed on ileal samples. Ethanol produced greater activities of the lipid-reesterifying enzymes in the jejunum than did glucose. Ileal specific activity of acyl-CoA synthetase was also increased in the experimental group. No effect of ethanol on jejunal disaccharidase enzyme activities was noted. It is concluded that ethanol given acutely has a specific stimulating effect on intestinal enzymes involved in lipid absorption.
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PMID:The effect of acute ethanol treatment on lipid-reesterifying enzymes of the rat small bowel. 116 87

Ethanol feeding to rats for 40 days enhanced (p < 0.001) the activities of alkaline phosphatase, sucrase, gamma-glutamyltransferase (GTP), and p-nitrophenyl (PNP)-beta-D-galactosidase (p < 0.05) with no change in leucine amino peptidase (LAP) and PNP-beta-D-glucosidase activities in intestine compared with control rats. The activities of alkaline phosphatase, sucrase, and GTP were diminished (p < 0.01) in ethanol-fed malnourished rats. There was no change in LAP activity, but the levels of glucosidase and galactosidase were elevated under these conditions. Brush-border sialic acid, fucose, hexose, and hexosamine contents were elevated in ethanol-fed protein-deficient animals. Ethanol administration to normally fed rats elevated the membrane sialic acid and hexose contents, reduced fucose content, and had no effect on brush-border hexosamine content compared with the control group. These results are in agreement with data on lectin binding to brush borders under these conditions. Alcohol ingestion reduced the incorporation of [14C]-glucosamine into brush borders in rats maintained on an 18% protein diet but augmented the incorporation of [14C]-glucosamine and [14C]-mannose in protein-malnourished membranes. These observations suggest that nutrition status influences the sensitivity of microvillus membrane glycosylation to ethanol feeding in rat intestine.
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PMID:Chronic ethanol feeding and microvillus membrane glycosylation in normal and protein-malnourished rat intestine. 142 85

Phytomonas sp. isolated from Euphorbia characias was adapted to SDM-79 medium. Cells isolated in the early stationary phase of growth were analyzed for their capacity to utilize plant carbohydrates for their energy requirements. The cellulose-degrading enzymes amylase, amylomaltase, invertase, carboxymethylcellulase, and the pectin-degrading enzymes polygalacturonase and oligo-D-galactosiduronate lyase were present in Phytomonas sp. and were all, except for amylomaltase, excreted into the external medium. Glucose, fructose and mannose served as the major energy substrates. Catabolism of carbohydrates occurred mainly via aerobic glycolysis according to the Embden-Meyerhof pathway, of which all the enzymes were detected. Likewise, the end-products of glycolysis, acetate and pyruvate, glycerol, succinate and ethanol were detected in the culture medium, as were the enzymes responsible for their production. Mitochondria were incapable of oxidizing succinate, 2-oxoglutarate, pyruvate, malate and proline, but had a high capacity to oxidize glycerol 3-phosphate. This oxidation was completely inhibited by salicylhydroxamic acid. No cytochromes could be detected either in intact mitochondria or in sub-mitochondrial particles. Mitochondrial respiration was not inhibited by antimycin, azide or cyanide. The glycolytic enzymes, from hexokinase to phosphoglycerate kinase, and the enzymes glycerol kinase, glycerol-3-phosphate dehydrogenase, phosphoenolpyruvate carboxykinase, malate dehydrogenase and adenylate kinase, were all associated with glycosomes that had a buoyant density of about 1.24 g cm-1 in sucrose. Cytochemical staining revealed the presence of catalase in these organelles. The cytosolic enzyme pyruvate kinase was activated by fructose 2,6-bisphosphate, typical of all other pyruvate kinases from Kinetoplastida. The energy metabolism of the plant parasite Phytomonas sp. isolated from E. characias resembled that of the bloodstream form of the mammalian parasite Trypanosoma brucei.
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PMID:Characterization of carbohydrate metabolism and demonstration of glycosomes in a Phytomonas sp. isolated from Euphorbia characias. 143 59

To examine the effects of prenatal exposure to ethanol on postnatal development of small intestinal and liver functions, female rats were accustomed to increasing amounts of ethanol (10 to 25%, vol/vol) in tap water for 1 mo. During pregnancy, ethanol-fed dams had higher daily caloric intake and similar weight gain compared with controls. In ethanol offspring, neonatal mortality was 28.9% compared to 0% in controls. Although ethanol had been withdrawn at birth, pups issued from ethanol-treated mothers showed at 5 and 10 d postpartum decreased values of body weight, jejunal and ileal weights, and intestinal DNA concentration per unit of length, as well as lower specific and total activities in lactase and maltase, compared with controls. DNA synthesis rates, measured by the incorporation of [3H]thymidine into mucosal DNA, were also significantly (-20 to -34%, p < 0.01) depressed in the jejunum and ileum of ethanol pups at 5 and 10 d of age. All these parameters returned to control levels by d 15 postpartum. Electron microscopy of jejunal mucosal samples at 5, 10, and 15 d of age revealed that ethanol pups differed from controls by a fetal-like immature aspect of the enterocytes, which persisted up to d 15. The ontogenic upsurge in sucrase and the decline in lactase occurred at weaning with the same chronology in both groups, but the level reached by sucrase activity was about 50% lower in alcohol offspring than in controls. Except for moderate steatosis, the ultrastructure of hepatocytes was unaltered in sucklings.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Prenatal exposure to ethanol in rats: effects on postnatal maturation of the small intestine and liver. 148 Apr 59

Saccharomyces cerevisiae regulatory genes CAT1 and CAT3 constitute a positive control circuit necessary for derepression of gluconeogenic and disaccharide-utilizing enzymes. Mutations within these genes are epistatic to hxk2 and hex2, which cause defects in glucose repression. cat1 and cat3 mutants are unable to grow in the presence of nonfermentable carbon sources or maltose. Stable gene disruptions were constructed inside these genes, and the resulting growth deficiencies were used for selecting epistatic mutations. The revertants obtained were tested for glucose repression, and those showing altered regulatory properties were further investigated. Most revertants belonged to a single complementation group called cat4. This recessive mutation caused a defect in glucose repression of invertase, maltase, and iso-1-cytochrome c. Additionally, hexokinase activity was increased. Gluconeogenic enzymes are still normally repressible in cat4 mutants. The occurrence of recombination of cat1::HIS3 and cat3::LEU2 with some cat4 alleles allowed significant growth in the presence of ethanol, which could be attributed to a partial derepression of gluconeogenic enzymes. The cat4 complementation group was tested for allelism with hxk2, hex2, cat80, cid1, cyc8, and tup1 mutations, which were previously described as affecting glucose repression. Allelism tests and tetrad analysis clearly proved that the cat4 complementation group is a new class of mutant alleles affecting carbon source-dependent gene expression.
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PMID:Extragenic suppressors of yeast glucose derepression mutants leading to constitutive synthesis of several glucose-repressible enzymes. 200 6


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