Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To investigate the role of soyabean trypsin inhibitor (TI) during rotavirus (RV) diarrhoea, changes in enzyme activities of six relevant mucosal enzymes (lactase, sucrase, maltase, trehalase, glucoamylase and alkaline phosphatase) were assayed following inoculation of suckling mice with EB rotavirus (serotype 3) along with the TI and compared with the age-matched healthy control mice. The animals were divided into three groups i.e. group 1 (controls), group 2 (RV inoculated) and group 3 (RV + TI inoculated and sacrificed under light anaesthesia on 0, 1, 3, 5, 7 and 10 day post inoculation (dpi). Then intestines were excised and divided into two parts (jejunum and ileum). They were separately homogenized in 0.9% cold normal saline and activities of mucosal enzyme were measured. Alkaline phosphatase and disaccharidases were found to be decreased significantly in RV inoculated animals in both the anatomical portions of small intestine of mice. These enzyme levels were restored with the administration of TI i.e. in group 3 and became comparable to the controls in both intestinal portions. These studies suggest that activity of intestinal enzymes which are important in digestive absorptive functions of small intestine were restored with the addition of TI whengiven to infant mice showing its protective efficacy during rotavirus infection.
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PMID:Protection against rotavirus diarrhoea in mice by trypsin inhibitor. 1256 17

The present study was planned to observe the effect of protein-energy malnutrition on the gastric and duodenal mucosa. The activities of digestive enzymes (i.e. lactase, sucrase, maltase, trehalase, glucoamylase, leucine aminopeptidase, alkaline phosphatase and gamma-glutamyl transpeptidase) from the gastric (fundus, body and antrum) and duodenal mucosa [i.e. first (D1) and second (D2) part of the duodenum] were determined in 6 control, 6 protein-energy malnourished (PEM) and 6 rehabilitated young rhesus monkeys. There was a significant increase in the activity of the lactase enzyme in the antrum, and D1 and D2 portions of the duodenum of PEM monkeys, while the activity of all other enzymes was significantly increased in the D1 and D2 portions only. The increase in the activity of the above-mentioned enzymes became normal upon rehabilitation. There was no change in the enzyme activities of the gastric mucosa in mild-to-moderate PEM states. This study demonstrates that even mild-to-moderate malnutrition states affect the activity of enzymes in the gastric and duodenal mucosa. Enzyme activity recovers on rehabilitation.
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PMID:Effect of malnutrition on the digestive enzymes of the upper gastrointestinal tract of young rhesus monkeys. 1297 10

The aim of the present study was to investigate the effect of mild-to-moderate protein-energy malnutrition (PEM) and rehabilitation on the digestive enzymes of the large bowel in young rhesus monkeys. The presence of these enzymes has already been reported in the large bowel by many authors. The activities of the digestive enzymes, i.e. lactase, sucrase, maltase, trehalase, glucoamylase, leucine aminopeptidase, alkaline phosphatase and gamma-glutamyl transpeptidase, from different parts of the large bowel were determined in 6 controls, 6 PEM and 6 rehabilitated young rhesus monkeys. These monkeys had been used to study the effect of malnutrition on the small intestine and the results have already been published. There was a significant decrease in the sucrase in the ascending colon (p < 0.05); maltase in all the parts of the large bowel (p < 0.05); and glucoamylase activities (p < 0.05) in the caecum segment of the large bowel in the PEM group. The activity of other enzymes, i.e. lactase, trehalase, alkaline phosphatase, gamma-glutamyl transpeptidase and leucine aminopeptidase, was unaffected in the PEM group. The changes in the enzyme activities recovered on rehabilitation of 21 weeks. The result of this study suggest that even mild-to-moderate malnutrition affects the enzyme activity of the large bowel, which recovers on rehabilitation.
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PMID:Effects of malnutrition on the digestive enzymes of the large bowel of young rhesus monkeys. 1516 29

The effect of carbofuran administration to rats has been studied on enzymes functions in rat intestine. Carbofuran was administrated 4.0 mg/kg body weight for 7 days or 2.8 mg/kg body weight for 30 days daily by Ryle's tube. Animals given carbofuran for 30 days exhibited retarded growth compared to control group. The activities of sucrase (56%), alkaline phosphatase (62%), leucine aminopeptidase (56%), and gamma-glutamyl trans peptidase (84%) were enhanced in animals given carbofuran for 7 days. Enhancement in the activities of alkaline phosphatase and leucine amino peptidase (92-96%) was also observed in animals exposed to carbofuran for 30 days, but the activities of sucrase (28%) and gamma-glutamyl transpeptidase (49%) were reduced under these conditions. There was no change in activities of maltase, lactase, and trehalase in pesticide-treated animals for 7 or 30 days. The activity of lactate dehydrogenase was enhanced (p < 0.001) in 7 days and 30 days induced carbofuran toxicity. The activities of glucose-6-phosphatase and glutamate pyruvate transaminase were also enhanced (p < 0.001) in pesticide-treated animals for 7 days, but were reduced by 46% and 26%, respectively, after 30 days of carbofuran exposure. The activity of glutamate oxaloacetate transaminase was unaltered in carbofuran toxicity. Kinetic analysis of brush border enzymes revealed a change in V(max) with no change in apparent Km. Western blot analysis of brush border sucrase, alkaline phosphatase, and leucine aminopeptidase corroborated the enzyme activity data. Intestinal histological revealed distruption of the villi, and comet assay showed disintegration of DNA in enterocytes of animals exposed to carbofuran for 30 days. These findings suggest that carbofuran toxicity may modulate digestive functions in rat intestine.
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PMID:Subacute effects of carbofuran on enzyme functions in rat small intestine. 1977 59

ABSTRACT Iron is an essential element for biological systems. There is increasing evidence that excess iron supplementation results in the deposition of iron in the duodenum and enhances mucosal injury and cell proliferation in the colon and cecum. In the present study we examined whether chronic exposure to high levels of iron fortification affects the functional integrity of the small intestine, especially the activities of various brush border enzymes. Wistar rats were fed iron 29 mg/kg body weight (or 6.58 mg/kg Fe) daily in the form of FeSO(4).7H(2)O for 39 days. The activities of brush border alkaline phosphatase (AP) (p < 0.001), sucrase (p < 0.01), maltase (p < 0.05), lactase (p < 0.05), and trehalase (p < 0.001) were reduced in purified membranes in iron-fed animals compared to controls. However, the activities of leucine amino peptidase (LAP) and gamma-glutamyl transpeptidase (gamma-GTP) were unaffected under these conditions. Analysis of alkaline phosphatase activity across the crypt-villus unit revealed a significant decrease (p < 0.05) all across the crypt-villus length, while sucrase activity was reduced (p < 0.01) only in the midvillus axis in iron-exposed animals. Kinetic studies showed a decrease in V(max) of AP from 1.11 to 0.83 units/mg protein and for sucrase from 0.77 to 0.43 units/mg protein in iron-fed rats, with no change in the apparent K(m) of the enzymes (AP, 8 mM; sucrase, 10 mM). Western blot analysis corroborated these findings. These results indicate that chronic iron exposure alters the activities of brush border enzymes, resulting in intestinal dysfunctions.
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PMID:Effect of chronic iron ingestion on the development of brush border enzymes in rat intestine. 2002 Sep 42

The saliva of Rhynocoris marginatus consists of amylase, invertase, trehalase, protease, acid phosphatase, alkaline phosphatase, phospholipase, lipase, trypsin, hyaluronidase, and esterase. All enzyme activities were significantly higher in the saliva of female R. marginatus when compared to the saliva of male individuals. The saliva was analyzed by tricine SDS/PAGE, sephadex column chromatography, FT-IR, and MALDI-TOF. The pH of the saliva was slightly alkali. The SDS/PAGE revealed a few proteins with molecular masses greater than 29.5 and 36.2 kDa for male and female predator saliva respectively. The FT-IR spectrum confirmed the acidic, proteinaceous, enzymatic, and aromatic nature of the saliva. The MALDI-TOF-MS revealed the presence of enzymes, proteins, peptides, and other biomolecules. The most prominent peptides were named as RmIT-1 (3.79 kDa), RmIT-2 (9.7 kDa), and RmIT-3 (10.94 kDa) (Rhynocoris marginatus Insect Toxin). Further studies are underway to isolate and identify these biomolecules.
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PMID:Biochemical and electrophoretic analyses of saliva from the predatory reduviid species Rhynocoris marginatus (Fab.). 2351 91

Gluconobacter strains are specialized in the incomplete oxidation of monosaccharides. In contrast, growth and product formation from disaccharides is either very low or impossible. A pathway that allows growth on trehalose was rationally designed to broaden the substrate range of Gluconobacter oxydans. Expression vectors containing different signal sequences and the gene encoding alkaline phosphatase, phoA, from Escherichia coli were constructed. The signal peptide that exhibited the strongest periplasmic PhoA activity was used to generate a G. oxydans strain able to utilize the model disaccharide trehalose as a carbon and energy source by expressing the periplasmic trehalase TreA from E. coli. The strain had a doubling time of 3.7h and reached a final optical density of 1.7 when trehalose was used as a growth substrate. In comparison, the wild-type harboring the empty vector and the strain expressing treA without a signal sequence grew slowly to a final OD of only 0.15. The trehalose concentration in treA expressing cultures decreased continuously during the exponential growth phase indicating that the substrate was hydrolyzed to glucose by TreA. In contrast to the wild-type growing on glucose, the treA expression strain mainly formed acetate and 5-ketogluconate as end products rather than gluconate.
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PMID:Production of a periplasmic trehalase in Gluconobacter oxydans and growth on trehalose. 2517 74


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