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)

Acute experiments were conducted on ratlings; it was shown that the action of heat (40-41 degrees C), cold (5-6 degrees C), and ACTH injections (4 units per 100 g of body weight) during the first week after birth led to a sharp reduction of the total (alpha-gamma-conditioned) amylolytic and invertase activity of the homogenates and of the portions of the small intestine (turned inside out) of the growing rats. This depressed condition of the intestinal function was revealed directly after the arrest of the action of the unfavourable factors (7-day rats) and persisted for the subsequent two weeks of the animal life.
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PMID:[Effect of heat and cold on the amylolytic and invertase activity of the small intestine of growing rats]. 19 6

Mutants with defective carbon catabolite repression have been isolated in the yeast Saccharomyces cerevisiae using a selective procedure. This was based on the fact that invertase is a glucose repressible cell wall enzyme which slowly hydrolyses raffinose to yield fructose and that the inhibitory effects of 2-deoxyglucose can be counteracted by fructose. Repressed cells were plated on a raffinose--2-doexyglucose medium and the resistant cells growing up into colonies were tested for glucose non-repressible invertase and maltase. The yield of regulatory mutants was very high. All were equally derepressed for invertase and maltase, no mutants were obtained with only non-repressible invertase synthesis which was the selected function. A total of 61 mutants isolated in different strains were allele tested and could be attributed to three genes. They were all recessive. Mutants in one gene had reduced hexokinase activities, the other class, located in a centromere linked gene, had elevated hexokinase levels and was inhibited by maltose. Mutants in a third gene were isolated on a 2-deoxyglucose galactose medium and had normal hexokinase levels. A partial derepression was observed for malate dehydrogenase in all mutants. Isocitrate lyase, however, was still fully repressible.
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PMID:Mutants of Saccharomyces cerevisiae resistant to carbon catabolite repression. 19 90

To better understand the pathogenesis of infantile viral gastroenteritis, we studied Na+ and Cl- fluxes in vitro in short-circuited jejunal epithelium from 8-10-day-old piglets after infection with a standard dose of human rotavirus given via nasogastric tube. 11 infected piglets, all of whom became ill, were compared with 9 uninfected, healthy litter-mates. When killed 72 h after infection, intestinal villi were shorter and crypts deeper (P less than 0.025) in duodenum, upper jejunum, and mid-small intestine, but not ileum in infected piglets. Virus antigen was seen by fluorescence microscopy in occasional jejunal villus tip cells in only four infected piglets and no controls at 72 h. Net Na+ and Cl- fluxes did not differ from noninfected litter-mate controls under basal conditions, but response to glucose was blunted in infected piglets (P less than 0.001). Theophylline stimulated net Cl- secretion in both infected and control animals, and cyclic AMP concentration in isolated jejunal villus enterocytes did not differ significantly. In isolated jejunal villus enterocytes of infected piglets, thymidine kinase activity increased (P less than 0.001), and sucrase activity decreased (P less than 0.001). We conclude that in this invasive enteritis caused by a major human viral pathogen, glucose-coupled Na+ transport is impaired in the jejunum at a time when the villus epithelium shows enzyme characteristics of crypt epithelium, and when little or no virus is present. These findings are identical to those occurring in an invasive coronavirus enteritis of piglets but differ markedly from those seen with enterotoxigenic diarrhea.
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PMID:Human rotavirus enteritis induced in conventional piglets. Intestinal structure and transport. 19 22

In the genus Schizosaccharomyces intracellular osidases and nitrite and nitrate reductases are revealed; particularly all the species possessing invertase, alpha-glucosidase and alpha-galactosidase. These characters underline the homogeneity on the genus. On the basis of osidases, nitrite and nitrate reductases results, 2 groups can be distinguished in this genus.
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PMID:[Study of intracellular enzymes in the genus Schizosaccharomyces. Sistematic implications]. 19 42

In three profiles of a semi-gley soil under the floodplain forest, variations were studied in the activities of invertase, amylase, cellobiase, cellulase, proteases, and phosphatases. In the surface soil layer, enzymatic activity was found affected by the soil moisture at a significant level, whereas in the deeper soil layers the influence of aeration was more effective. Moreover, significant correlations could be detected between the amount of available nitrogen and protease activity, while the water-soluble phosphorus acted as a represeive agent on the activity of phosphatases. Existence of correlations between the numbers of microbes and enzymes could be demonstrated for invertase and protases only.
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PMID:Enzymatic activity in a semi-gley soil under the floodplain forest in South Moravia. 20 42

1. Stimulation of fluid secretion from fly salivary glands by 5-hydroxytryptamine (5-HT) is known to involve calcium and cyclic AMP. Isolated salivary glands were used to investigate the role of these second messengers in the control of enzyme (sucrase) secretion.2. The protein component of secretion from isolated glands treated with 5-HT appears to be identical to that of saliva secreted by flies during feeding.3. Stimulation of fluid secretion by 5-HT follows a definite dose-response curve, but there is no consistent relationship between the rate of enzyme secretion and the stimulating concentration of 5-HT.4. Exogenous cyclic AMP causes secretion of enzymes as well as of fluid, thus mimicking the action of 5-HT. The phosphodiesterase inhibitor theophylline enhances the rate of 5-HT-stimulated enzyme secretion.5. Removal of calcium from the bathing medium enhances enzyme secretion in response to 5 or 10 nM-5-HT but has no effect on enzyme secretion stimulated by 100 nM-5-HT or by cyclic AMP.6. Addition of 0.1 mM-lanthanum to medium containing 2 mM-calcium mimics the effect of calcium-free solution on 5-HT-stimulated enzyme secretion.7. The ionophore A 23187 causes secretion of both fluid and enzyme. The secretory rate is initially high but soon declines and ceases after about 40 min.8. Enzyme secretion in response to 5-HT or to cyclic AMP is progressively inhibited as the concentration of potassium is increased from 10 to 80 mM. Secretion in response to A 23187 is initially inhibited by 80 mM-potassium but then partially recovers.9. The rate of enzyme secretion appears to be affected by the intracellular concentrations of both calcium and cyclic AMP. It is possible that the rate of enzyme secretion increases as the intracellular calcium concentration rises, until the optimal calcium concentration is reached when further increase in the level of calcium progressively inhibits secretion. The optimal calcium concentration for enzyme secretion is lower than that for fluid secretion, and 5-HT normally causes maximal fluid secretion and submaximal enzyme secretion.
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PMID:The control of enzyme secretion from fly salivary glands. 20 76

Yeast mutants with glucose-insensitive formation of mitochondrial enzymes were isolated starting with a strain completely lacking alcohol dehydrogenase activity. The mutations could uniquely be attributed to a single nuclear gene, designated CCR80. They were largely dominant. Glucose-resistant enzyme formation was most prominent with regard to mitochondrial enzymes succinate dehydrogenase and NADH: cytochrome c oxidoreductase. The effect of CCR80r mutations was rather small but significant on the gluconeogenetic enzymes isocitrate lyase, malate synthase and fructose-1,6-bisphosphatase and on invertase synthesis. The repressive effect of maltose in CCR80r mutants was also reduced showing that glucose-resistance is not caused by a mere hexose uptake defect. This regulatory disorders were not accompanied by reduced levels of glycolytic enzymes or drastically altered levels of glycolytic intermediates. Aerobic fermentation of glucose was almost completely inhibited in the mutants; anaerobic glucose degradation was reduced but not completely abolished. Therefore, the mutants appear to be altered in the regulation of glycolysis. A largely glucose-resistant synthesis of respiratory enzymes is obviously a corollary of this alteration.
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PMID:A yeast mutant with glucose-resistant formation of mitochondrial enzymes. 20 62

The biological activity of the soil under a beech forest and a spruce forest was examined in respect to the CO2-production of the soil samples, the speed of vanillin decomposition, as well as the activity of the soil enzymes catalse, saccharase and phosphatase. Both soils indicated an indentical course of seasonal activity.
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PMID:[Seasonal changes in soil biological activity of two different forest association (author's transl)]. 20 61

Various enzyme activities involved in the active transport system, glycolysis, and digestion were assayed in various parts of the gastrointestinal tracts of germfree, conventional, and gnotobiotic rats associated with indigenous bacteria. The activity levels of alkaline phosphatase, glucose 6-phosphatase, adenosine triphosphatase, and disaccharidases in the upper small intestine were highest in all parts of the gastrointestinal tracts of various kinds of gnotobiotic, conventional, and germfree rats. Alkaline phosphatase, glucose 6-phosphatase, and adenosine triphosphatase activities in the upper small intestine of germfree rats were, respectively, 2.3-, 2.9-, and 1.7-fold higher than those in conventional rats. Similar to the results of these enzymes, sucrase, maltase, trehalase, and lactase activities in the upper small intestine of germfree rats were, respectively, 1.6-, 1.5-, 2.3-, and 1.8-fold higher than those in conventional rats. In various gnotobiotic rats, enzyme activity levels were intermediate between those in germfree and conventional rats. These findings suggest that those enzymatic activities are strongly depressed by the association with the indigenous microorganisms in the epithelial mucosa of the upper small intestine of rats. The levels of pyruvate kinase, hexokinase, and lactate dehydrogenase activities were highest, respectively, in the stomach, cecum, and the upper small intestine and cecum in all parts of the gastrointestinal tracts in various kinds of gnotobiotic, conventional, and germfree rats. It was also shown that six kinds of gastrointestinal bacteria, including lactobacilli, significantly depressed the enzyme activity levels to levels between those of the germfree and conventional rats in the upper small intestine of gnotobiotic rats.
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PMID:Intestinal enzyme activities in germfree, conventional, and gnotobiotic rats associated with indigenous microorganisms. 20 6

The rat small bowel was perfused in vivo and ex vivo in the absence of biliary and pancreatic secretion. Intraluminal release of sucrase, alkaline phosphatase, aminopeptidases and enterokinase was significantly increased after administration of pentagastrin, caerulein and glucagon at doses ranging between 1 pg and 10 microgram. This suggests that there is a direct hormonal stimulation of the intestinal mucosa. This effect might at least partly be mediated through cyclic AMP since dibutyryl derivates of this cyclic nucleotide exerted a significant stimulatory effect on intraluminal release of proteins, sucrase and enterokinase, although the pattern of enzyme was quite different from the effect produced by the three peptides.
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PMID:Hormonal stimulation of intestinal brush border enzymes release. 20 30


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