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:3.2.1.26 (invertase)
4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A procedure was developed for the analytical isolation of brush border and basal lateral plasma membranes of intestinal epithelial cells. Brush border fragments were collected by low speed centrifugation, disrupted in hypertonic sorbitol, and subjected to density gradient centrifugation for separation of plasma membranes from nuclei and core material. Sucrase specific activity in the purified brush border plasma membranes was increased fortyfold with respect to the initial homogenate. Basal lateral membrane were harvested from the low speed supernatant and resolved from other subcellular components by equilibrium density gradient centrifugation. Recovery of Na, K-ATPase activity was 94%, and 61% of the recovered activity was present in a single symmetrical peak. The specific activity of Na, K-ATPase was increased twelvefold, and it was purified with respect to sucrase, succinic dehydrogenase, NADPH-cytochrome c reductase, nonspecific esterase, beta-glucuronidase, DNA, and RNA. The observed purification factors are comparable to results reported for other purification procedures, and the yield of Na, K-ATPase is greater by a factor of two than those reported for other procedures which produce no net increase in the Na, K-ATPase activity. Na, K-ATPase rich membranes are shown to originate from the basal lateral plasma membranes by the patterns of labeling that were produced when either isolated cells or everted gut sacs were incubated with the slowly permeating reagent 35S-p-(diazonium)-benzenesulfonic acid. In the former case subsequently purified Na, K-ATPase rich and sucrase rich membranes are labeled to the same extent, while in the latter there is a tenfold excess of label in the sucrase rich membranes. The plasma membrane fractions were in both cases more heavily labeled than intracellular protein. Alkaline phosphatase and calcium-stimulated ATPase were present at comparable levels on the two aspects of the epithelial cell plasma membrane, and 25% of the acid phosphatase activity was present on the basal lateral membrane, while it was absent from the brush border membrane. Less than 6% of the total Na, K-ATPase was present in brush border membranes.
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PMID:Analytical isolation of plasma membranes of intestinal epithelial cells: identification of Na, K-ATPase rich membranes and the distribution of enzyme activities. 13 16

Brush border sucrase and lactase activities are significantly elevated in alloxan-induced chronic diabetes and are restored to control levels after insulin treatment. Alkaline phosphatase and Mg-ATPase levels remain unchanged in diabetes, compared to a control group. Insulin treatment alone to control animals also led to enhanced activities of these enzymes.
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PMID:Effect of chronic alloxan diabetes and insulin administration on intestinal brush border enzymes. 14 19

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

A genetically conditioned mouse model of exocrine pancreatic insufficiency (epi) has been used to study the effect of the absence of lumenal proteases on small intestinal mucosal proteins. The small bowel was divided into eight equal segments. Enzyme activity was increased only in the first three segments in the case of maltase, sucrase, and lactase (all mol wt above 200,000). Alkaline phosphatase (mol wt 145,000), trehalase (mol wt 95,000), and peptidase (mol wt 175,000) activities were unaffected in proximal segments from epi mice. Proximal brush border proteins were identified and measured quantitatively by sodium dodecyl sulfate acrylamide gel electrophoresis. Those enzymes with increased activity were associated with increased amounts of protein in epi mice. Double labeled studies of protein turnover revealed a longer half-life for large brush border proteins (mol wt above 175,000) in epi mice than in normal mice. Enterokinase activity (a marker for duodenal mucosa) was nearly absent from the duodenum of epi mice. Receptors for the intrinsic factor-vitamin B12 complex (markers for ileal mucosal) were present in the ileum equally in normal and in epi mice. Enterokinase activity can be induced in epi mice by feeding its substrate trypsinogen, but not by trypsin or chymotrypsinogen. Epi mice thus retain the ability to synthesize enterokinase. Pancreatic proteases play an important role in the turnover of certain large mucosal proteins and in the induction of enterokinase.
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PMID:Effect of exchange exocrine pancreatic insufficiency on small intestine in the mouse. 20 83

The activities of rat intestinal enzymes, sucrase, lactase, maltase, trehalase, gamma-glutamyltransferase, leucylnaphthylamide-hydrolyzing activity, and the transport system for glucose follow diurnal rhythms on ad libitum and restricted feeding regimes. In response to 6 days of restricted feeding, food available between 1400 and 1800 Eastern Standard Time, all rhythms shifted in time and the daily levels of activities were changed. Alkaline phosphatase activity followed a diurnal rhythm only in restricted fed animals. In restricted fed rats several activity patterns were observed, some with short periods of maximum activity, 3 h or less, and some with plateaus of maximum activity, 5-9 h long. In respect to the time of day of the synchronizer, sucrase peaked before feeding, glucose transport peaked during feeding, alkaline phosphatase peaked after feeding, and the other enzymes had higher levels of activity before, during and after feeding. The effect of restricted feeding on the daily activity levels were: a decrease in leucylnaphthylamide-hydrolyzing activity, no change in alkaline phosphatase, and increases in the others. These enzyme and transport systems exhibit a large amount of individual regulation or control as reflected by the lack of a uniform activity pattern and response to the synchronizer, and the variation in direction and magnitude of the adaptations to restricted feeding.
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PMID:Effect of changes in feeding schedule on the diurnal rhythms and daily activity levels of intestinal brush border enzymes and transport systems. 24 Apr 40

The activities of ornithine aminotransferase, sucrase and acid and alkaline phosphatases have been studied throughout sporulation in Saccharomyces cerevisiae. The same enzymes were monitored during synchronous vegetative growth. Each of these enzymes has been demonstrated to increase in a 'step' manner during both growth and sporulation. Alkaline phosphatase increased in a two-step manner whereas the others increased in a single step. The times of increase of these enzymes formed a similar sequence during both sporulation and growth. It has been proposed that these enzymes are under a common mechanism of control during growth and sporulation and that the sequence of enzyme appearance may be used as markers of the sporulation process.
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PMID:The use of step enzymes as markers during meiosis and ascospore formation in Saccharomyces cerevisiae. 37 Mar 42

1. The proteins of the intestinal microvillus membrane have been studied during post-natal development in the rat (days 12--37). 2. In suckling animals (up to age 20 days), the majority of alkaline phosphatase, glucoamylase and lactase activities in the distal half of the intestine were located in the supernatant fraction (100000 X g, 60 min). These enzymes were attached to the membrane from the proximal intestine at all ages. 3. Alkaline phosphatase, maltase and lactase activities in the supernatant fractions chromatographed in Sephadex G-200 in positions similar to the corresponding membrane enzyme. Corresponding activities for lysosomal counter-parts of maltase and lactase present in the supernatant fraction chromatographed differently. Moreover, pH optimum of the soluble enzymes was 9.2 for phosphatase and 5.5--6.0 for glycoamylase and lactase. The soluble lactase and alkaline phosphatase were inhibited minimally by p-chloromercuribenzoate, and sodium fluoride respectively. L-Phenylalanine (20 mM) did inhibit the soluble phosphatase by 90%. Thus, the soluble enzymes are not mainly of the lysosomal origin, but have characteristics of membrane-bound enzymes. 4. Polyacrylamide gel electrophoresis in sodium dodecyl sulfate revealed 18 protein bands which were present in adult membranes. Two other proteins were unique for membranes of distal intestine in suckling rats. The proteins corresponding to known enzyme activity changed as expected with age (e.g. sucrase, maltase increased, lactase decreased). Most of the other proteins were also altered in amount during development. Thus, the changes in the microvillus membrane during development in the rat are not limited to specific enzymes.
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PMID:Development of intestinal brush border membrane proteins in the rat. 41 9

1. Rats were fed with the elemental diet Vivonex for 1 or 3 months and their jejunal histology was compared with that of an equal number of rats fed on a normal diet. 2. After 1 month of Vivonex feeding a significant reduction in the ratio of crypt height: villus height (CH:VH) was found in the Vivonex-fed rats (n = 4) compared with the control rats (n = 4) (P less than 0.05). 3. After 3 months the CH:VH ratio was also reduced in the Vivonex-fed rats (n = 18) compared with control rats (n = 18) (P less than 0.002). Villus height was significantly increased (P less than 0.002) and crypt height decreased (P less than 0.05). 4. Jejunal protein content, alkaline phosphatase and disaccharidase activity were also determined in 12 control and 12 Vivonex-fed rats from the 3 months study. 5. Alkaline phosphatase activity was increased from a control value of 201 +/- 8 to 243 +/- 15 munits/cm in the Vivonex-fed rats (n = 12) (P less than 0.05) but no significant changes in lactase, sucrase or maltase activites were found. The observed decrease in the CH:VH ratio suggested an improved survival of the mature enterocyte population during elemental diet feeding.
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PMID:Small-intestinal changes induced by an elemental diet (Vivonex) in normal rats. 72 6

A modification of Weiser's (1973) cell isolation method was used in order to study the developmental pattern of various intestinal enzyme activities in villus and crypt cells of normal rats from 5 days after birth until 8 weeks. Alkaline phosphatase and enterokinase activities were always located in the upper villus zone during postnatal development. Enterokinase activity was higher in the upper villus cells during the third week of life than after this period. Aminopeptidase activity was located in the crypt cells during the first week, its maximum activity remained in this area until the third week. At this time, sucrase activity appeared in the crypt cells, then aminopeptidase and sucrase activities rose to the villus zone during the fourth week. Amylase activity was detected along the entire crypt-villus axis 5 days after birth, reaching maximum activity in crypt cells at the end of the first week and in the upper villus cells after the fourth week. In contrast with the other enzymes studied almost all amylase activity was soluble in the youngest animals whereas at weaning most of the activity appeared in a particulate form in the villus cells. But in the crypt cells the ratio between particulate and soluble form remained unchanged until the adult stage. Various hypotheses are advanced to explain the patterns of evolution of the different enzymes.
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PMID:Intestinal enzymes activities in isolated villus and crypt cells during postnatal development of the rat. 83 93

Lactase and cellobiase were detectable in the fetal intestine by the 3rd month of gestation, and although there was little change by the 9th month, maximal levels were reached at birth and steadily declined after 4 months. Conversely maltase, sucrase and trehalase were barely discernible in the fetus, maltase being present at low levels at birth, but all increased during the suckling period to attain adult levels by 7 months of age. Alkaline phosphatase activity matured earlier than did disaccharidase activity. Mucosal enzymes other than alkaline phosphatase were virtually absent from meconium and the large intestine. Continued ingestion of lactose could be detrimental in foals suffering from severe diarrhoea.
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PMID:The development and distribution of mucosal enzymes in the small intestine of the fetus and young foal. 106 Aug 71


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