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)

The survival and prognosis of the prematurely born human infant are dependent on a successful transition from the intrauterine to the extrauterine environment. This is largely a consequence of the maturation of sufficient gastrointestinal function to provide adequate nutrition. However, the gastrointestinal tract of the premature infant, and to some extent, of the full-term infant, may be unprepared to provide the requisite absorptive function. Data presented in this symposium emphasize the dissociations in the development of human gastrointestinal function. Morphological maturation is completed early in gestation while glucose absorption increases with gestational age. Sucrase and maltase activities appear early; lactase activity begins to increase at 30 weeks and increases steadily to term. The latter pattern is accompanied by increased production of cortisol and thyroid in the fetus. The intraluminal phase of fat digestion is immature even in the full-term neonate. Both pancreatic secretory function and bile salt metabolism mature postnatally. Despite this relative immaturity, breast milk fat is absorbed with great efficiency by the term infant, and breast milk provides other important influences on intestinal development: mitogenic factor, immunological support, control of intestinal flora. The goals of nutrition support of the premature infant have been to maintain intrauterine growth standards; yet premature infants receiving pooled breast milk from mothers at 40 weeks or more may be given too little protein for their needs. Human milk from mothers of premature infants may be a more appropriate nutrient source. Supplements with higher contents of amino acids may lead to amino acid imbalance or hyperammonaemia. Additional stresses and requirements are imposed by illness or congenital anomalies. While we must apply current research findings to clinical care, we must also extend our knowledge of extrauterine human development. The ultimate measure of success in this field will be the physical and neurological capacities of infants followed prospectively.
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PMID:The immature intestine: implications for nutrition of the neonate. 9 85

1. The elution profiles of eleven acid hydrolases from human liver and plasma were directly compared using a system whereby a single salt gradient was simultaneously applied to two DEAE-cellulose chromatographic columns. 2. Plasma alpha-L-fucosidase, alpha-mannosidase, alpha-galactosidase and alpha-glucosidase isoenzymes were eluted at higher salt concentrations than the corresponding liver isoenzymes whereasbeta-N-acetylglucosaminidase, beta-galactosidase, beta-glucosidase, exo-1,4-beta-xylosidase and alpha-L-arabinofuranosidase isoenzymes were eluted at lower salt concentrations. The elution profiles of beta-glucuronidase and acid phosphatase weremore complex. 3. After incubation with neuraminidase most plasma hydrolases were eluted at lower salt concentrations, however the elution patterns of beta-glucosidase, beta-xylosidase and acid phosphatase were not altered. 4. Preincubation with neuraminidase had no effect on the elution profiles of six liver hydrolases whereas the major isoenzymes of alpha-mannosidase, beta-galactosidase and alpha-L-arabinofuranosidase were eluted at markedly lower salt concentrations. Liver alpha-fucosidase and alpha-galactosidase were eluted at slightly lower salt concentrations afterincubation with neuraminidase. 5. The results are discussed in relation to thepathogenesis of Mucolipidosis II (I-cell disease), and the synthesis and packaging of lysosomal enzymes.
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PMID:Effect of neuraminidase on the chromatographic behaviour of eleven acid hydrolases from human liver and plasma. 19 Dec 58

To determine whether oxytetracycline hydrochloride and the sodium salt of ampicillin have any adverse effects on the rat intestine, enteric enzyme levels and glucose transport rates were measured in vitro in rats. The intestinal transport of glucose did not differ significantly between control animals and those pretreated with ampicillin. For animals pretreated with oxytetracycline, the transport rates were significantly lower than those for the control group. The difference between the ampicillin and oxytetracycline groups, however, was not statistically significant. No significant differences in enteric levels of sucrase and maltase activity were found between any of the groups. The possibility that some antimicrobial agents may interfere with the absorption of nutrients suggested the need for caution in using these drugs in experimental animals.
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PMID:The effects of selected antimicrobials on glucose transport in the rat intestine. 37 63

Mutants (NP1 and PSJ5) of Tetrahymena thermophila strains B and D 1968 exist that are unable to construct a functional oral apparatus and form food vacuoles at 37 C but which do so normally at 30 C. Food vacuole-less cells starved in dilute salt solution released similar amounts of acid phosphatase, beta-N-acetyl-glucosaminidase and alpha-glucosidase activity into the medium as wildtype cells during an 8-h period. Actively growing, food vacuole-less cells had approximately 50% less total protein, acid phosphatase, beta-N-acetyl-glucosaminidase, and alpha-glucosidase per cell than wildtype cells after 72-h growth. During this time food vacuole-less cells released significant amounts of the 3 acid hydrolases into the growth medium. For each hydrolase, the total activity released from growing, food vacuole-less cells was less, on a per cell basis, tahn the amount released from food vacuole formers. The proportion of the total activity secreted by the mutant and the wildtype cells was the same for acid phosphatase and beta-N-acetyl-glucosaminidase and somewhat lower for alpha-glucosidase. It is concluded that the release of a significant amount of acid hydrolase activity from Tetrahymena is independent of food vacuole formation and may be analogous to the secretory activity of other nonphagocytic eukaryotic cells.
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PMID:Acid hydrolases and their release in food vacuole-less mutants of Tetrahymena thermophila. 39 96

The effect of intestinal bacterial over-growth on brush border hydrolases and brush border glycoproteins was studied in nonoperated control rats, control rats with surgically introduced jejunal self-emptying blind loops, and rats with surgically introduced jejunal self-filling blind loops. Data were analyzed from blind loop segments, segments above and below the blind loops, and three corresponding segments in the nonoperated controls. Rats with self-filling blind loops had significantly greater fat excretion than controls and exhibited significantly lower conjugated:free bile salt ratios in all three segments. Maltase, sucrase, and lactase activities were significantly reduced in homogenates and isolated brush borders from the self-filling blind loop, but alkaline phosphatase was not affected. The relative degradation rate of homogenate and brush border glycoproteins was assessed by a double-isotope technique involving the injection of d-[6-(3)H]glucosamine 3 h and d-[U-(14)C]glucosamine 19 h before sacrifice, and recorded as a (3)H:(14)C ratio. The relative degradation rate in both homogenate and brush border fractions was significantly greater in most segments from rats with self-filling blind loops. In the upper and blind loop segments from rats with self-filling blind loops, the (3)H:(14)C ratios were higher in the brush border membrane than in the corresponding homogenates, indicating that the increased rates of degradation primarily involve membrane glycoproteins. Incorporation of d-[6-(3)H]glucosamine by brush border glycoproteins was not reduced in rats with self-filling blind loops, suggesting that glycoprotein synthesis was not affected. Polyacrylamide gel electrophoresis of brush border glycoproteins from the contaminated segments indicated that the large molecular weight glycoproteins, which include many of the surface hydrolases, were degraded most rapidly. Brush border maltase, isolated by immunoprecipitation, had (3)H:(14)C ratios characteristic of the most rapidly degraded glycoproteins. The results indicate that bacteria enhance the destruction of intestinal surface glycoproteins including disaccharidases. Since alkaline phosphatase, a glycoprotein, is not affected, the destruction is selective and presumably involves only the most exposed membrane components.
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PMID:Pathogenesis of mucosal injury in the blind loop syndrome. Brush border enzyme activity and glycoprotein degradation. 41 Aug 30

Mitochondrial and microsomal fractions were isolated from guinea pig myocardium by differential pelleting. The mitochondrial fraction was subjected to analytical subfractionation by sucrose density gradient centrifugation and the gradient fractions assayed for marker enzymes for the various mitochondrial compartments, viz outer membrane (monoamine oxidase), intermembranous space (adenylate kinase), inner membrane (Mg2+-dependent ATPase and cytochrome c oxidase) and mitochondrial matrix (malate dehydrogenase), and for creatine kinase. Both creatine kinase and adenylate kinase were released by suspending the mitochondria in 50 mmol . litre-1 sodium phosphate buffer. Sonication or disruption with the detergent, digitonin released the adenylate kinase but the creatine kinase remained associated with the inner membranes. Subsequent salt treatment desorbed the creatine kinase from these membranes. It is concluded that creatine kinase is located to the outer aspect of the inner mitochondrial membrane. Analytical subfractionation of the microsomal fraction clearly resolved markers for the sarcolemma (5'-nucleotidase), outer mitochondrial membrane (monoamine oxidase) and endoplasmic reticulum (neutral alpha-glucosidase and RNA). Creatine kinase was localised in the endoplasmic reticulum particularly the smooth membranes.
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PMID:Sub-mitochondrial and sub-microsomal distribution of creatine kinase in guinea pig myocardium. 51 58

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

Extracts from Xenopus eggs capable of nuclear envelope assembly in vitro were fractionated by differential and density gradient centrifugation. Nuclear envelope assembly was found to require soluble components in the cytosol and two distinct particulate fractions, which we have called nuclear envelope precursor fractions A and B (NEP-A and NEP-B). Both NEP-A and NEP-B are sensitive to treatments with trypsin, sodium carbonate, and detergents, but can be distinguished from each other by their sensitivities to high salt and N-ethylmaleimide and by their levels of alpha-glucosidase activity. Vesicles in NEP-B bind to chromatin, whereas those in NEP-A do not. NEP-B may therefore be involved in the targeting of membranes to the surface of the chromatin, whereas NEP-A may provide a pool of vesicles that contributes many of the nuclear envelope membranes. NEP-B may also play a role in the assembly of nuclear pore complexes because the density of nuclear pores in the resulting envelope is dependent on the ratio of NEP-B to NEP-A in the reconstituted extract.
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PMID:A distinct vesicle population targets membranes and pore complexes to the nuclear envelope in Xenopus eggs. 199 30

Initiated by the recently published histochemical method for the investigation of alfa-D-galactosidas with an indoxyl substrate, the current state of this group of synthetic compounds in light and electron microscopic histochemical glycosidase research is evaluated whereby historical, functional, methodological and applied aspects are considered. Beginning with the introduction of indoxyl acetate for non-specific esterase in 1951 and 1952 numerous other indoxyl substrates and mostly substituted in the 5- and 4-position of the indol ring by Br and Cl were developed to study histochemically non-specific phosphatases and glycosidases and frequently used in indigogenic, azoidoxyl, tetrazolium salts and metal salt techniques for catalytic (activity) histochemical and less often for immunohistochemical, affinity histochemical and hybridohistochemical purposes. The last substrate which became available and was validated for activity histochemistry was 5-Br-4-Cl-3-indoxyl alfa-1-galactoside for alfa-1-galactosidase. At present, the indoxyl glycosides are more widely used than 5-Br-4-Cl-3-indoxyl acetates and phosphates when compared with the alternative synthetic (artificial) naphthol, 6-Br-2-naphthol or ternative synthetic (artificial) naphthol, 6-Br-2-naphthol AS substrates, and among the indoxyl glycosides those for the oxoglycosidases lactase, maltase-glucoamylase, glucoamylase, acid beta-D-galactosidase, neuroaminidase and alfa-D-galactosidase are superior to other artificial compounds. When one considers in addition, electron microscopic catalytic glicosidase histochemistry (ultracytochemistry, 5-Br-4-Cl-3-indoxyl is the only suitable moiety for this purpose. These glycosidase can mostly be localized in plasma membranes or lysosomes and also measured there in tissue sections but are also found in secretion granules, endoplasmic reticulum and organ lumina.
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PMID:Indoxyl alfa-D-galactoside as the temporarily last substrate for glycosidase histochemistry. The present state of the art in histochemical glycosidase research using indoxyl glycosidas. 209 81

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


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