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)

The activities of various glycosidases in homogenates of the small intestinal mucosa of two adult and 18 suckling tammar wallabies (M. eugenii) aged from 6 to 50 weeks were investigated. Lactase (beta-D-galactosidase), beta-N-acetylglucosaminidase, alpha-L-fucosidase and neuraminidase activities were high during the first 34 weeks post partum and then declined to very low levels. Maltase, isomaltase, sucrase and trehalase activities were very low or absent during the first 34 weeks, and then increased. The lactase activity was unusual in being greater in the distal than the middle or proximal thirds of the intestine, and in its low pH optimum (pH 4.6), inhibition by p-chloromercuribenzene sulfonate but not by Tris, and lack of cellobiase activity. These properties are those of a lysosomal acid beta-galactosidase rather than of a brush border neutral lactase. The maltase activity had the characteristics of a lysosomal acid alpha-glucosidase early in lactation and of a brush border neutral maltase in adult animals. The significance of these findings is discussed in relation to changes in dietary carbohydrates during weaning and to the mode of digestion of milk carbohydrates by the pouch young.
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PMID:Intestinal lactase (beta-galactosidase) and other glycosidase activities in suckling and adult tammar wallabies (Macropus eugenii). 678 21

Jejunal sucrase is known to display glucocorticoid responsiveness from birth through day 17 but not beyond that age. The aim of the current study was to determine whether this abrupt loss of responsiveness was shared by maltase, lactase, and acid beta-galactosidase. Glucocorticoid concentrations were manipulated by both adrenalectomy (ADX) and by administration of cortisone acetate (CA). Surgery or treatment was performed on each day from 16--22 days of age. Maltase activity was reduced by ADX at day 18 and earlier and was increased by CA at days 16 and 17. There were no effects at later ages. Acid beta-galactosidase was increased by ADX only at day 18 and earlier and was decreased by CA only at day 16. Lactase activity was increased by ADX at all ages up to and including day 20 but was reduced by CA only at days 16 and 17. Thus, we conclude that loss of glucocorticoid responsiveness at a relatively early stage of development is a common feature of both brush-border and lysosomal enzymes of the small intestine.
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PMID:Coordinate loss of glucocorticoid responsiveness by intestinal enzymes during postnatal development. 680 95

Female rats of the Wistar strain, weighing 40-60 g were used to study the effect of fish meals (Coryphaenoides rupestris, Chimaera monstruosa and Merluccius merluccius) on the disaccharidases and alkaline phosphatase in the small intestine in relation to the control group which consumed casein. Fish meal diets diminished lactase and alkaline phosphatase activity, the latter being most remarkable in animals fed Ch. monstruosa meal, while no statistical variations in maltase and sucrase activity were observed. Maltase, sucrase and lactase activity of animals fed Ch. monstruosa meal dropped in comparison with those fed C. rupestris meal, while the alkaline phosphatase activity showed no significant changes.
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PMID:[Effect of various fish meals on disaccharidases and alkaline phosphatase of the small intestine in rats]. 681 26

The relation between food intake and enzyme activity of the small intestine and rate of intestinal absorption were studied in rats 15 days after induction of alloxan diabetes. Diabetic rats were given an ad lib. semisynthetic diet or a restricted diet on the basis of either daily intake or body weight. The rates of absorption of 5 mMD-galactose and L-valine were determined in vitro by the everted sac method. The rates of absorption of the substances, expressed per unit weight or per length of intestine, were higher in diabetic rats than in controls, regardless of the amount of food consumed. Maltase and sucrase activities were significantly increased in diabetic rats, regardless of the amount of food consumed. The activity of intestinal alkaline phosphatase was increased in diabetic rats fed ad lib., but not in those on a restricted diet. These findings suggest that in alloxan diabetic rats the increased disaccharidase activity in the small intestine is due to insulin deficiency, and that the increased activity of alkaline phosphatase is only a secondary effect of insulin deficiency, caused by increased food intake resulting from insulin deficiency.
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PMID:Effect of food intake on intestinal absorption and mucosal hydrolases in alloxan diabetic rats. 698 35

The effect of four raw legume diets: field beans (Vicia faba) (RFB), navy beans (Phaseolus vulgaris) (RNB), soybeans (Glycine soja) (RSB) and bitter vetch (VICIA ervilia) (RBV), on disaccharidase activities in chick small intestine have been studied. Maltase and sucrase activities, which vary with age, were determined in 1 to 60 day old animals, RFB and RBV diets had no effect on maltase activity and only increased sucrase activity in 60 day old chicks. Both maltase and sucrase activities decreased in chicks on RSB diet, regardless of their age, and the decrease was even more pronounced in chicks on RNB diet. Contrarywise, chicks fed on autoclaved navy beans and soybeans showed a considerably higher activity of these disaccharidases.
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PMID:Effect of raw legume diets on disaccharidase activity in the small intestine of chicks. 719 9

The effect of vitamin C deficiency on the digestive and absorptive functions of the gut has been investigated in guinea pigs. The absorption of D-glucose was significantly elevated, but that of L-leucine, L-alanine and L-lysine considerably depressed in the intestine of scorbutic guinea pigs compared to controls. The intestinal transport of vitamin B12 was also diminished. Activities of sucrase and alkaline phosphatase on the brush border were enhanced, but that of leucine aminopeptidase markedly reduced in scorbutic animals compared to controls. Maltase activity was unaffected in vitamin C deficient animals. Chemical analysis of the brush borders isolated from scorbutic animals revealed a considerable decrease in membrane protein, total lipids, phospholipids, and free cholesterol contents compared to control animals. In vivo 2-(14)C-acetate incorporation into membrane lipids suggested that the observed decrease in lipid components of the scorbutic membranes is due to reduced synthesis. Administration of ascorbic acid to scorbutic animals ameliorated the intestinal aberrations observed in scurvy.
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PMID:Effect of vitamin C deficiency in guinea pigs on intestinal functions and chemical composition of brush border membrane. 730 86

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

Brush border enzymatic activities (maltase, lactase and sucrase) have been determined in the ileal mucosa of rats subjected to a 30% ethanol ingestion for 3 and 5 months. The data were compared with the results obtained with control rats. Mucosal protein content after 3 months of ethanol treatment was similar to that of control rats. Maltase, lactase and sucrase specific activities in ileal mucosa were significantly decreased in ethanol-fed animals as compared to control rats. After 5 months of ethanol consumption, the protein content was decreased in ethanol-fed rats. However, no differences were found between specific activities of maltase, lactase and sucrase of ethanol-fed with respect to control rats. It is suggested that prolonged exposure of rats to ethanol results in adaptive responses to the effects of shorter periods of exposure on intestinal mucosal function.
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PMID:Changes in the ileal disaccharidase activities in rats after long-term ethanol feeding. 867 76

In three experiments broiler chickens were inoculated with sporulated Eimeria acervulina oocysts at 18 d of age. Feed intake, body-weight gain, brush-border enzyme activities, fat digestion, protein digestion and protein retention were measured. Body-weight gain was reduced during the acute phase of the infection and increased during the recovery phase of the infection. Feed intake was decreased on day 4 and day 5 postinfection (PI) and increased from day 7 to day 11 PI. Maltase (EC 3.2.1.20) and sucrase (EC 3.2.1.48) activities were decreased on day 5 PI in all intestinal segments. In Expts 2 and 3, however, maltase activity was increased in the ileum. Fat digestion was decreased from day 2 to day 11 PI. N digestion and retention were decreased from day 2 to day 11 PI.
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PMID:Interaction between nutrition and Eimeria acervulina infection in broiler chickens: development of an experimental infection model. 877 31

Non-physiological amounts of oral polyamines have been reported to induce precocious gut maturation in rat pups. The aim of the present study was to investigate organ distribution and metabolic fate of orally administered stable-isotopically labelled polyamines in rat pups. Pups received tetradeuterium-labelled putrescine (Pu-d4; 3 mumol), spermidine (Sd-d4; 5 mumol), spermine (Sp-d4; 3 mumol), or physiological saline twice daily on postnatal days 7-10 or 12-15. They were killed on days 10 and 15. We determined activities of ileal lactase (EC 3.2.1.23), maltase (EC 3.2.1.20), sucrase (EC 3.2.1.48) and diamine oxidase (EC 1.4.3.6) and established villus and crypt lengths. Polyamines and their labelling percentages in organs were determined by GC and mass fragmentography. Treatments did not affect growth rate, but caused lower weights of liver, kidneys and heart. Maltase activity increased, lactase decreased, whereas sucrase and diamine oxidase did not change. Villus and crypt lengths increased. Organ polyamine pools were labelled to different extents. Irrespective of the orally administered polyamine, all organs contained Pu-d4, SD-d4 and Sp-d4. Administered Pu-d4 and Sd-d4 were recovered mainly as Sd-d4, whereas Sp-d4 was recovered as Sp-d4 and Sd-d4. Total polyamines in a caecum, colon and erythrocytes increased, but increases were only to a minor extent with regard to labelled polyamines. Our data confirm precocious gut maturation by exogenous polyamines. Putrescine appears to be limiting factor. The exogenous polyamines were distributed among all investigated organs. They are not only used for the synthesis of higher polyamines, but also retroconverted to their precursors. Changes in erythrocyte polyamine contents suggest precocious stimulation of erythropoiesis.
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PMID:Oral administration of deuterium-labelled polyamines to sucking rat pups: luminal uptake, metabolic fate and effects on gastrointestinal maturation. 938 89


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