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)

Feeding sodium deoxycholate orally to rats for four days caused depression of the activity of the small intestinal enzymes lactase, sucrase, maltase, alkaline phosphatase, and N-acetyl-beta-glucosaminidase. The first four are brush border enzymes, the last a lysosomal enzyme. Alkaline phosphatase activity recovered very rapidly and rebounded to above the normal level within 24 hours. The activity of the three disaccharidases returned to normal within seven days while no recovery was observed within 96 hours of the activity of the lysosomal enzyme, N-acetyl-beta-glucosaminidase, after removing the bile salt from the diet.
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PMID:Deoxycholate depresses small-intestinal enzyme activity. 114 Jun 27

A subcellular fractionation method to isolate simultaneously apical and basolateral plasma membrane fractions from the human adenocarcinoma cell line Caco-2, grown on filter supports, is described. The method employs sucrose-density-gradient centrifugation and differential precipitation. The apical membrane fraction was enriched 14-fold in sucrase-isomaltase and 21-fold in 5'-nucleotidase compared with the homogenate. The basolateral membrane fraction was enriched 20-fold relative to the homogenate in K(+)-stimulated p-nitrophenylphosphatase. Alkaline phosphatase was enriched 15-fold in the apical membrane fraction and 3-fold in the basolateral membrane fraction. Analytical density-gradient centrifugation showed that this enzyme was a true constituent of both fractions, and experiments measuring alkaline phosphatase release following treatment with phosphatidylinositol-specific phospholipase C showed that in both membrane fractions the enzyme was glycosyl-phosphatidylinositol-linked. There was very little contamination of either membrane fraction by marker enzymes of the Golgi complex, mitochondria or lysosomes. Both membrane fractions were greater than 10-fold purified with respect to the endoplasmic reticulum marker enzyme alpha-glucosidase. Protein composition analysis of purified plasma membrane fractions together with domain-specific cell surface biotinylation experiments revealed the presence of both common and unique integral membrane proteins in each plasma membrane domain. The post-synthetic transport of endogenous integral plasma membrane proteins was examined using the devised subcellular fractionation procedure in conjunction with pulse-chase labelling experiments and immunoprecipitation. Five common integral membrane proteins immunoprecipitated by an antiserum raised against a detergent extract of the apical plasma membrane fraction were delivered with the same time course to each cell-surface domain.
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PMID:The post-synthetic sorting of endogenous membrane proteins examined by the simultaneous purification of apical and basolateral plasma membrane fractions from Caco-2 cells. 131 18

Lactase, maltase, sucrase, and alkaline phosphatase activities were determined in the intestinal mucosa from 3 locations in the small intestine and 4 locations in the large intestine 1 year after extensive large-colon resection (group 1; n = 5) and 1 year after sham operation (group 2; n = 3) in horses. Lactase, maltase, and sucrase activities were similar (P greater than 0.05) between group-1 and group-2 horses in all locations measured in the intestinal tract. Alkaline phosphatase activity in the remaining large colon of group-1 horses was significantly (P less than 0.05) greater than the activity in the large colon of group-2 horses. Decreased apparent digestion of phosphorus and a negative phosphorus balance are persistent features of large-colon resection in horses. Increases in alkaline phosphatase activity in the remaining colon of horses with extensive large-colon resection may be a specific functional adaptive mechanism that attempts to counteract the derangements in phosphorus metabolism.
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PMID:Alteration of intestinal enzyme activities associated with extensive large-colon resection in horses. 211 42

1. Brush border membrane vesicles were prepared from lamb enterocytes. These were used to study the changes in the enzyme contents and the transport capacities which occur during the change from a milk to a roughage diet. 2. Na+-dependent transport of D-glucose was present in all regions of the small intestine of pre-ruminant lambs and absent in ruminants. 3. Na+-dependent transport of L-proline was present in all regions of the small intestine irrespective of the age of the animal. 4. Phosphate transport was seen only in the presence of a transmembrane pH gradient (acid outside). The transport was not stimulated by either Na+ or K+. The transport capacity increases 2-fold as the animal becomes ruminant. 5. The activities of lactase and maltase diminished with age. Alkaline phosphatase and aminopeptidase N activities remain constant. Sucrase activity cannot be detected in lambs of any age.
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PMID:Changes in the functions of the intestinal brush border membrane during the development of the ruminant habit in lambs. 251 73

We examined the age-related changes of renal brush border enzymes of male Donryu rats under different dietary conditions. High protein diet (51% casein) markedly decreased the activity of renal leucine aminopeptidase as compared with low protein diet (8% casein). No significant difference, however, was observed in the activity of renal maltase between high and low protein diets. Alkaline phosphatase activity from young adult (3-month-old) rats in the high protein diet group was significantly lower than that in the low protein diet groups. From these results, it is inferred that dietary conditions affect the age-related alteration of renal brush border enzymes. Together with the previous results, it is suggested that proteins of renal brush borders are altered differently during the aging process.
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PMID:Age-related changes in brush border enzymes under different dietary conditions. 265 43

The fetal and postnatal activity patterns of different hydrolytic enzymes (alkaline phosphatase, gamma-glutamyltransferase, trehalase, maltase, glucoamylase, lactase, and sucrase) have been examined in mouse renal homogenates. Alkaline phosphatase and gamma-glutamyltransferase activities presented approximately similar changes. They increased from 18 days of gestation up to 30 days after birth. These activities showed marked increases during the 3rd and 4th postnatal weeks. A similar important rise was observed for trehalase activity at the end of the suckling period. Maltase activity increased gradually after birth. Traces of lactase, sucrase, and glucoamylase activities were detected at each developmental stage.
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PMID:[Activity of renal hydrolases in pre- and postnatal development of mice]. 286 26

Alkaline treatment of proteins leads to chemical changes which alter the proteins' digestibility. Severely alkali-treated casein (0.2N NaOH, 80 degrees C, 1 hour) in the diet reduces food intake and growth of young but not of adult Sprague Dawley rats. Gastrointestinal transit time is not reduced significantly in either young or adult rats. Food intake and growth rate are improved by amino acid supplementation. In this case, protein content and total leucine aminopeptidase activity are increased in the distal part of the small intestine whereas gamma-glutamyl-transpeptidase and maltase activities are increased in both the proximal and distal parts. Alkaline phosphatase activity remains unchanged. These intestinal adaptations differ from those observed in rats receiving a diet containing untreated casein and graded levels of a synthetic trypsin inhibitor. In the latter, protein digestibility remains high, gamma-glutamyltranspeptidase and also maltase activities are increased in the proximal and medial parts of the small intestine only. Intestinal adaptation in rats receiving alkali-treated casein does not result from a deficiency of pancreatic proteases activity. Ileal accumulation of undigested peptides from insufficient hydrolysis of alkali-treated casein may account for these mucosal adaptations.
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PMID:Effect of severely alkali-treated casein on gastrointestinal transit and selected intestinal enzyme activities. 287 20

Effects of non lethal concentrations of hexavalent chromium on intestinal enzymology of Salmo gairdneri and Dicentrarchus labrax (Pisces). The effects of an exposure to potassium dichromate on intestinal enzyme activities (Alkaline phosphatase, maltase, leucine amino peptidase and ATPases) have been studied on a fresh water fish (Salmo gairdneri) and a salt water fish (Dicentrarchus labrax). Fish were exposed at seasonal temperatures (13 or 21 degrees C) to toxic concentrations equal to 1/10 of the 24 h-LC 50 (i.e. 18 mg/l Cr for trout and 5 mg/l Cr for bass) during respectively 13 and 21 days. Intoxicated trout stopped feeding and showed a decrease in their intestinal weight at the end of the experiments. A decrease of brush border membrane activities (Alkaline phosphatase, maltase and leucine amino peptidase) were also observed. These alterations have been interpreted as the consequence of the chromium induces fasting. Intoxicated bass showed no alterations of their feeding habits. Two specific effects of chromium on enzyme activities have been found: a severe decrease of the alkaline phosphatase activity and an increase of the Na/K ATPase activity. These enzyme activities could be useful indicators of chromium intoxication in marine fish.
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PMID:[Effects of hexavalent chromium at non-lethal concentrations on the enzymology of the intestine of Salmo gairdneri and Dicentrarchus labrax (Pisces)]. 297 85

We previously have shown that aging alters the expression of several intestinal enzymes during cell migration from the crypt base to the villus tip. The activities of many mucosal enzymes are dramatically altered by starvation and refeeding. We compared the effects of starvation and refeeding on the activities of selected intestinal enzymes in young and aging Fischer 344 rats. Gut mass fell during starvation and rose during refeeding to a similar extent in both groups. Sucrase and maltase specific activities in control aging rats were lower than in young controls and, during starvation, enzyme activities declined at approximately similar rates in both groups. Total duodenal enzyme activities fell by about two-thirds in young animals and by greater than 80% in aged animals. Alkaline phosphatase and adenosine deaminase activities also were lower in aging than young animals. During refeeding, enzyme activities rose more in aging rats than in the young. In fact, the specific activities of sucrase and maltase in aging rats refed for 1 day exceeded the values found in fed aging controls. The adaptive responses of duodenal enzymes exceeded those in the jejunum. In conclusion, the aging intestine responds appropriately to starvation and refeeding. However, the fluctuations in brush-border enzyme activities are much greater in aging than in young rats. Such alterations may be an important influence of aging on gut differentiation and might have an adverse impact upon nutritional maintenance in aging animals.
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PMID:Adaptive changes of intestinal enzymes to nutritional intake in the aging rat. 359 66

Jejunal segments from fetal rats of 18 days gestation were maintained in an organ culture system for up to 72 h. During this period, villi developed within the intestinal lumen and the epithelium changed from stratified to simple columnar. Peristaltic activity was observed during in-vitro culture. Alkaline phosphatase specific activity of the bowel segments fell after 48 hours culture, compared with pre-culture values (P less than 0.05), but that of alpha-glucosidase increased. The addition of Frazer's gluten fraction III to the culture medium caused slowing in the rate of morphological maturation of the jejunal explants, but there was no additional effect on enzyme specific activities compared with segments cultured in gluten-free medium. The place of organ culture of fetal rat intestine as an animal model for testing cereal toxicity in the study of coeliac disease remains unclear.
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PMID:Organ culture of fetal rat small intestine for testing gluten toxicity: a reappraisal. 381 99


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