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

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Query: EC:3.2.1.20 (alpha-glucosidase)
4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Studies have been done on the effect of Penicillin, Streptomycin and Isonicotinic Acid hydrazide on small intestinal oligosaccharidase and it was observed that the drug penicillin inhibited the enzyme lactase and sucrase by 62.7% and 34.7% respectively, whereas I.N.H. inhibited the enzyme sucrase and maltase by 57.1% and 56.14% respectively. Streptomycin did not show any inhibitory effect on those enzymes. Lactose tolerance test showed impairment of lactose absorption in case of penicillin. Fasting serum sugar level was diminished both in penicillin and streptomycin and the absorption capacity was increased after oral administration of streptomycin.
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PMID:Studies on the effect of penicillin, streptomycin and isonicotinic acid hydrazide on small intestinal oligosaccharidase. 115 32

In 63 infants and children with a histological normal mucosa of the duodenum, without an isolated defect of enzyme and with a normal increase of xylose and glucose in serum after a combined xylose-lactose loading test the activities of disaccharidases were log normal distributed. The asymmetric distributions were transformed into symmetric ones and the geometric mean (x) as well as the range (+/- 2 s) of maltase, saccharase, isomaltase, lactase and trehalase were calculated. Only the activity of lactase shows a significant dependency on age. In the first year of age the lower limit (x -- 2 s) of this enzyme is much higher than later.
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PMID:[Disaccharidases of the small intestine mucosa in infants and children. "Normal values", log normal distribution and age dependence]. 122 50

Enzymatic modification at the nonreducing end D-glucosyl residue of p-nitrophenyl alpha-maltopentaoside was developed by using the transglycosylation of beta-D-galactosidase from Bacillus circulans. The enzyme regioselectively synthesized p-nitrophenyl 4(5)-O-beta-D-galactosyl-alpha-maltopentaoside (a yield of 12.0% based on the amount of p-nitrophenyl alpha-maltopentaoside added) on a preparative scale from lactose as a donor and p-nitrophenyl alpha-maltopentaoside as an acceptor. It revealed that the nonreducing end galactosyl group of p-nitrophenyl 4(5)-O-beta-D-galactosyl-alpha-maltopentaoside did not prohibit the action of human salivary and pancreatic alpha-amylases. This derivative was shown to be very suitable as a novel substrate for analytical use of human alpha-amylase assay in serum through a conjugated reaction involving glucoamylase and alpha-D-glucosidase.
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PMID:Enzymatic synthesis of p-nitrophenyl 4(5)-O-beta-D-galactosyl-alpha-maltopentaoside as a substrate for human alpha-amylases. 137 91

Intestinal lactase activity in mammals is high at birth but begins to decline around weaning and reaches very low levels in adult life. The triggering mechanism for this decline is not clear. Because of the association of the decline with weaning, lack of lactose in the diet has been implicated. In 110 growing rats, the effect of continued supplementation of the diet after weaning with physiological amounts of either cows' milk or a 5% lactose solution on intestinal lactase and other disaccharidase enzyme activities was investigated. In both control and test animals, the specific lactase activity decreased from a peak value of 115 +/- 4 mumol min-1 g-1 protein before weaning to about 10% at maturity. There was no significant difference in the level or the pattern of decline between the groups. Sucrase, maltase and trehalase showed the normal maturational changes without being affected by the test diets. The finding suggests that diet, particularly the presence or absence of physiological amounts of lactose, has no appreciable effect on the age related spontaneous decline of intestinal lactase activity or on the pattern of development of the other disaccharidases.
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PMID:The effect of continued feeding of physiological amounts of lactose on the level of intestinal lactase and other disaccharidase enzyme activities in the rat. 211 Nov 52

A retrospective analysis was made of jejunal biopsies performed on 62 patients with Crohn's disease for disaccharidase levels and routine histology. Thirteen patients with irritable bowel syndrome acted as a control group. Two patients with Crohn's disease had hypolactasia. Two patients had marginally low sucrase levels, but all patients had normal maltase levels. Only one patient with irritable bowel syndrome had hypolactasia with normal histology. There were no significant differences between the two groups. Four patients with Crohn's disease had abnormal jejunal histology. The prevalence of hypolactasia in patients with Crohn's disease is not increased. Ideally lactase deficiency in patients with Crohn's disease should be confirmed before starting a lactose-free diet which can produce further restrictions on dietary intake.
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PMID:Hypolactasia and Crohn's disease: a myth. 211 83

Nucleic acid synthesis in tissues of rapid growth is preferentially done using dietary purines and pyrimidines via the salvage pathway. In the case of a low protein intake, dietary nucleotides may be semiessential for cell replication of gut, lymphocytes, and bone marrow, and especially in those intestinal diseases in which the mucosa is altered, dietary nucleotides may have a role in intestinal development. The effect of dietary nucleotides on intestinal weight and length, gut mucosal weight, intestinal protein and DNA contents, and lactase, maltase, and intestinal mucosal activities was assessed in a controlled way. Weanling (21-day-old) rats were separated into two groups of 36, each receiving blindly a basal diet containing glucose polymers (C) or a basal diet with lactose as the main carbohydrate (L) for 15 days. Those fed with L developed a syndrome of chronic diarrhea and malnutrition. Ten rats of each group were sacrificed at that time. The rest of the animals of each group were separated into two subgroups. The first was fed with the C diet and the second with the C diet supplemented with 50 mg/100 g of each of the following nucleotides: AMP, GMP, CMP, UMP, and IMP (CN). Thus the subgroups CC, CN, LC, and LN were formed. Rats were sacrificed after 4 weeks and gut separated into three segments corresponding to duodenum, jejunum, and ileum. Analysis of variance was used to compare the effect of diet or segments. DNA and lactase, maltase, and sucrase activities increased in the LN group with respect to LC especially in jejunum and ileum but there were not any differences between CC and CN.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effect of dietary nucleotides on intestinal repair in rats with experimental chronic diarrhea. 212 43

1. Tests for glycosidases were performed in homogenates of Brachionus plicatilis. 2. Hydrolytic activity was detected with the following substrates: (a) with synthetic substrates (NP = 4-nitrophenyl): NP-alpha- and NP-beta-D-glucopyranoside, NP-alpha- and NP-beta-D-galactopyranoside, NP-N-acetyl-beta-D-glucosaminide, NP-N-acetyl-beta-D-galactosaminide, NP-alpha- and NP-beta-D-mannopyranoside and NP-alpha-L-fucopyranoside; (b) with disaccharides: sucrose, maltose, trehalose, isomaltose, cellobiose, gentiobiose and lactose; (c) with polysaccharides: laminarine, carboxymethyl-cellulose, avicel, Micrococcus luteus (for lysozyme) and 4-nitrophenyl-alpha-D-maltoheptaoside (for amylase). 3. The pH dependence of the glycosidase activities was determined. 4. The distribution of enzyme activities within fractions from the homogenate was studied in order to localize them within the cell. 5. Proteins from Brachionus homogenate were separated by SDS-gel electrophoresis and the positions of the following glycosidase activities were detected by assays performed on the gels (estimated molecular weights in parentheses): alpha-glucosidase (250,000); beta-glucosidase (200,000); beta-galactosidase (70,000); N-acetyl-beta-glucosaminidase (60,000).
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PMID:Glycosidases in Brachionus plicatilis (Rotifera). 232 73

The effect of chronic intragastric infusion of hypertonic mannitol on small intestinal mucosal structure and function was studied in adult rats. Animals were gavage-fed 20% mannitol (1300 mosm) at a dose of 5 ml/100 g body weight daily for seven days. Control animals were gavage-fed tap water on the same schedule. On day 8, the animals were anesthetized, the duodenum cannulated, and a test sugar (glucose, glucose polymer, lactose, sucrose, or maltose) was infused at a dose of 0.5 g/kg body weight in 2.5 ml distilled water over less than 1 min. Portal vein glucose was measured at 30-min intervals from 0 to 120 min. Mannitol treatment resulted in histologic and biochemical alterations (reduced lactase, sucrase, maltase) limited to the proximal small intestine compared to the control group. The absorption of glucose and glucose polymers was similar in mannitol-treated and control animals. In contrast, digestion and absorption of lactose, sucrose, and maltose was significantly diminished in mannitol-treated animals when compared to controls. No changes in permeability to polyethylene glycol 4000 or Na+-coupled glucose transport were observed in mannitol-treated animals compared to controls. These data suggest that when the intestinal mucosa is exposed to hyperosmolar loads that the digestive capacity for disaccharides is suppressed more than its glucose absorptive capacities. Furthermore, glucose oligomers may be more readily digested and absorbed than disaccharides, in this setting, due, in part, to the proximal injury and less pronounced proximal-distal gradient for glucoamylase than other brush-border carbohydrases.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Proximal small intestinal mucosal injury. Maintenance of glucose and glucose polymer absorption, attenuation of disaccharide absorption. 249 65

Lactase-phlorizin hydrolase, a small intestinal disaccharidase, has been considered mainly an enzyme important only for the hydrolysis of lactose. After weaning in most mammals lactase-specific activity falls markedly, and, functionally, adult mammals are considered to be lactase deficient. However, the persistence of low levels of lactase activity in adulthood has never been explained. In addition, it has been suggested that lactase-phlorizin hydrolase is associated with glycosylceramidase activity when the enzyme is prepared by column chromatography, but it is unclear whether this represents copurified activities or two catalytic sites on one peptide. The developmental patterns of lactase-phlorizin hydrolase and other disaccharidases were investigated in homogenates of total rat small intestine; lactase and several glycosylceramidases were measured in immunoprecipitates from these homogenates using a monoclonal antibody. The developmental pattern of total lactase activity showed a steady 2.3-fold increase to adult levels (specific activity decreased eightfold), whereas total phlorizin-hydrolase activity increased 10.7-fold (specific activity decreased threefold). As expected, levels of both total and specific sucrase and maltase activities increased during development. In lactating rats total lactase activity showed a significant increase compared with adult males. The developmental pattern of the enzyme activities for the glycolipid substrates was similar to that found for lactase, and the immunoprecipitated enzyme showed a 40- to 55-fold higher affinity for the glycolipids than for lactose. Galactosyl- and lactosylceramide inhibited lactose hydrolysis by 38%, without a competitive pattern, suggesting two different active sites for lactose and glycolipid hydrolysis, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:New insights into lactase and glycosylceramidase activities of rat lactase-phlorizin hydrolase. 250 86

Small-intestinal disaccharidase activities of eight suckling T. vulpecula, aged from 34 to 150 days, and of two adult animals were investigated. Intestinal maltase, isomaltase and sucrase activities increased with age, whereas lactase activities decreased. Trehalase activities were relatively high in all animals and showed no obvious age-related changes. Three separate beta-galactosidase activities, one neutral and two acid, acted on lactose. The neutral beta-galactosidase activity appeared to be due to a brush border enzyme similar to that of eutherian mammals, whereas the acid beta-galactosidases were soluble and probably of lysosomal origin. One of these, acid beta-galactosidase-1, had similar properties to the sole intestinal beta-galactosidase of macropodid marsupials, whereas the other, acid beta-galactosidase-2, has not previously been described. Galactosyl oligosaccharides isolated from macropodid milk were readily hydrolysed by both acid beta-galactosidases but not by the neutral beta-galactosidase. The total intestinal lactase activity in animals aged up to 125 days was due mainly to acid beta-galactosidase-1, whereas in older animals it was due mostly to the neutral beta-galactosidase; this suggests that late in lactation the young T. vulpecula change from a macropodid mode of digestion of galactosyl oligosaccharides to a eutherian mechanism for the digestion of lactose. These findings may have implications for the hand-rearing of orphaned T. vulpecula.
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PMID:Intestinal lactase (beta-galactosidase) and other disaccharidase activities of suckling and adult common brushtail possums, Trichosurus vulpecula (Marsupialia:Phalangeridae). 251 66


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