Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.20 (alpha-glucosidase)
 4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Maternal vitamin D deficiency has been shown to lead to reduced body weights in developing rat pups. To evaluate the effects of vitamin D deficiency alone both in dams and pups during the perinatal age on the ontogeny of gastrointestinal enzymes, female weanling rats (3 weeks of age) were divided into three groups. Groups I and II were fed a control (vitamin-D-replete) diet. Group II were fed a vitamin-D-deficient diet. Six weeks afterward they were mated with normal male rats while continuing on their respective diets until sacrifice. Only rats that delivered their pups on the same day from each group were brought into the study. Litter sizes of groups I and II were adjusted to 10, while group III was adjusted to 13 such that the rate of growth paralleled that of group II. At 19 days after birth, all dams and pups were sacrificed. There were no differences in the calcium and phosphorus contents in breast milk obtained from dams of each group. The serum calcium concentration of pups from group II (vitamin-D-deficient) was lower than the other groups. Body weights of pups from groups II and III were significantly lower than those of group I. The mucosal weight, total mucosal protein, mucosal DNA, sucrase, and maltase activities from groups II and III were similar, but lower than group I. Pancreatic weight, total pancreatic protein, DNA, amylase, and lipase activities from groups II and III were also similar, but lower than group I. Vitamin D deficiency was confirmed in both dams and pups from group II.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Vitamin D deficiency, pancreatic and small intestinal enzyme development in rats. 320 79

Cell-associated oligo-1,6-alpha-glucosidase (EC 3.2.1.10) was isolated from Thermoanaerobium Tok6-B1 grown on starch-containing medium. Activity was purified 11.4-fold by salt precipitation, gel filtration, hydroxyapatite and anion-exchange chromatography. Molecular mass was determined as 30,000 by SDS/polyacrylamide-gel electrophoresis and 33,000 by analytical gel filtration. The probable order of specificity was p-nitrophenyl-alpha D-glucose greater than-isomaltose greater than-isomaltotriose greater than-panose greater than-nigerose and no activity was shown against malto-oligosaccharides, melezitose, melibiose, raffinose, cellobiose, sophorose, gentiobiose, lactose, pullulan, dextran or amylose. The optima for activity and stability were between pH 5.6 and 7.0 and the half-life at pH 6.5 was 1000 min at 70 degrees C and 20 min at 76 degrees C. Activity was stabilized by substrate, Mg2+, Mn2+ and Ca2+, but was destabilized by Zn2+ and EDTA. N-Ethylmaleimide, glucose and 1-O-methyl-alpha D-glucose were inhibitory but 1-O-methyl-beta D-glucose stimulated activity. The activation energy (Ea) was 109 kJ/mol.
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PMID:A cell-associated oligo-1,6-alpha-glucosidase from an extremely thermophilic anaerobic bacterium, Thermoanaerobium Tok6-B1. 321 28

Oral administration of Gossypol acetic acid (10 mg/kg body wt./day, daily for 15 days), an experimental antifertility agent to male rats, caused significant reduction in the uptake of glucose, alanine, leucine and calcium in the small intestinal segments. Gossypol also caused significant decrease in the intestinal brush border membrane--associated enzymes, sucrase, lactase, maltase and alkaline phosphatase. Kinetic analysis indicated that Gossypol decreased the apparent velocity of the disaccharidases while the Km was not altered. It also caused a shift in the transition temperature in these enzymes and predictably changed the energy of activation both below and above the transition temperature, although the Arrhenius expressions of the temperature dependence still showed proximity and were parallel to the control group.
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PMID:Effects of gossypol acetic acid on the absorptive and digestive functions of rat intestine. 324 43

We studied 24 patients with end-stage chronic renal failure not treated with hemodialysis (CRF1) and 16 patients on regular hemodialysis (CRF2), to investigate the digestive, absorptive and morphological aspects of the small intestinal mucosa. Serum d-xylose test and biochemical parameters of absorption (serum calcium and proteins) were determined. Jejunal mucosal biopsies were obtained and tissue homogenates assayed for disaccharidases (sucrase, maltase and lactase) and dipeptidases (glycyl-glycinase, leucyl-glycinase and leucyl-aminopeptidase). Histological changes were classified according to the severity of abnormality and compared with biopsies obtained from control subjects. Serum d-xylose test, calcium and proteins were normal in patients with CRF. Maltase specific activity was higher in CRF1 than in controls (p less than 0.05). Lactase and leucyl-aminopeptidase showed a tendency to decrease in CRF, but this difference did not reach statistical significance. Sucrase, glycyl-glycinase and leucyl-glycinase specific activity in CRF was similar to the control group. Histological changes of the small intestinal mucosa of mild to moderate degree were noted in 68% of patients with CRF vs 36% in control subjects (p less than 0.01). No significant difference was noted in the incidence of absorptive, enzymatic (with the exception of maltase) and histological changes between the two groups of patients with CRF. These changes are not influenced by hemodialysis, a long-term treatment averaging 6 months, they appear to represent primary manifestations of CRF and may be related to the nutritional status of patients with CRF.
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PMID:Small intestinal function and structure in patients with chronic renal failure. 339 24

An asialoglycoprotein receptor was isolated from murine liver and purified more than 1600-fold using 2-fold affinity chromatography on asialoorosomucoid-Sepharose. The purified receptor did not interact with 125I-orosomucoid, but bound to 125I-asialoorosomucoid. The binding of the receptor to asialoorosomucoid was saturable. The dissociation constant of the receptor-asialoorosomucoid complex was 0.4 X 10(-9) M. The molecular mass of the receptor, as determined with the use of specific antibodies by the immunoblotting method, was 43 kDa. High concentrations of unlabeled asialoorosomucoid and of n-aminophenyl-beta-D-galactosyl derivatives of bovine serum albumin, ovalbumin and acid alpha-glucosidase from human liver inhibited the binding of the receptor to 125I-asialoorosomucoid almost completely. The binding of the receptor to 125I-galactolyzed alpha-glucosidase was pH-dependent, with the pH optimum at 8.0-9.0. It was shown that, as in the case of 125I-asialoorosomucoid, the binding of the 125I-galactosyl derivative of alpha-glucosidase occurred in the presence of Ca2+ and was inhibited by N-acetylgalactosamine. Glycoproteins containing galactose as a terminal residue inhibited the interaction of the receptor with 125I-galactolyzed alpha-glucosidase. The possibility of directed transport of the galactolyzed alpha-glucosidase derivative into parenchymous liver cells using receptor-mediated endocytosis is discussed.
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PMID:Interaction of hepatic asialoglycoprotein receptor with asialoorosomucoid and galactolyzed lysosomal alpha-glucosidase. 352 76

Mouse epidermal growth factor/urogastrone (EGF/UG), administered sc in a dose of 0.1 microgram/g BW twice daily for 3 days, increased intestinal weight per unit length, lactase specific activity, and net calcium transport in normal 2-week-old suckling rats, but had no effect on maltase or sucrase specific activity. In normal 3-week-old weanling rats, the intestinal function of which is essentially fully mature, EGF/UG had no effect. These results suggest that EGF/UG, either secreted endogenously or ingested in breast milk, may have a role in both the morphological and functional maturation of the suckling rat intestine.
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PMID:Effect of mouse epidermal growth factor/urogastrone on the functional maturation of rat intestine. 640 26

The biogenesis of three intestinal microvillar enzymes, maltase-glucoamylase (EC 3.2.1.20), aminopeptidase A (aspartate aminopeptidase, EC 3.4.11.7) and dipeptidyl peptidase IV (EC 3.4.14.5), was studied by pulse-chase labelling of pig small-intestinal explants kept in organ culture. The earliest detectable forms of the enzymes were polypeptides of Mr 225000, 140000 and 115000 respectively. These were found to represent the enzymes in a 'high-mannose' state of glycosylation, as judged by their susceptibility to treatment with endo-beta-N-acetylglucosaminidase H (EC 3.2.1.96). After about 40-60 min of chase, maltase-glucoamylase, aminopeptidase A and dipeptidyl peptidase IV were further modified to yield the mature polypeptides of Mr 245000, 170000 and 137000 respectively, which were expressed at the microvillar membrane after 60-90 min of chase. The fact that the enzymes before reaching the microvillar membrane were found in a Ca2+-precipitated membrane fraction (intracellular and basolateral membranes), but not in soluble form, indicates that during biogenesis maltase-glucoamylase, aminopeptidase A and dipeptidyl peptidase IV are transported and assembled in a membrane-bound state.
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PMID:Biosynthesis of intestinal microvillar proteins. Pulse-chase labelling studies on maltase-glucoamylase, aminopeptidase A and dipeptidyl peptidase IV. 640 73

Lactobacillus acidophilus IFO 3532 was found to produce only intracellular alpha-glucosidase (alpha-D-glucoside glucohydrolase; EC 3.2.1.20). Maximum enzyme production was obtained in a medium containing 2% maltose as inducer at 37 degrees C and at an initial pH of 6.5. The enzyme was formed in the cytoplasm and accumulated as a large pool during the logarithmic growth phase. Enzyme production was strongly inhibited by 4 microM CuSO4, 40 microM CoCl2, and beef extract; MnSO4 and the presence of proteose peptone and yeast extract in the medium greatly enhanced enzyme production. A 16.6-fold purification of alpha-glucosidase was achieved by (NH4)2SO4 fractionation and DEAE-cellulose column chromatography. The enzyme showed high specificity for maltose. The Km for alpha-p-nitrophenyl-beta-D-glucopyranoside was 11.5 mM, and the Vmax for alpha-p-nitrophenyl-beta-D-glucopyranoside hydrolysis was 12.99 mumol/min per mg of protein. The optimal pH and temperature for enzyme activity were 5.0 and 37 degrees C, respectively. The enzyme activity was inhibited by Hg2+, Cu2+, Ni2+, Zn2+, Ca2+, Co2+, urea, rose bengal, and 2-iodoacetamide, whereas Mn2+, Mg2+, L-cysteine, L-histidine, Tris, and EDTA stimulated enzyme activity. Transglucosylase activity was present in the partially purified enzyme, and isomaltose was the only glucosyltransferase product. Amylase activity in the purified preparation was relatively weak, and no isomaltase activity was detected.
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PMID:Production and properties of alpha-glucosidase from Lactobacillus acidophilus. 641 77

The effect of vitamin D status on the topography of intestinal cell membranes was studied in isolated brush borders, as well as their purified membranes, by limited proteolysis. Addition of papain to brush borders isolated from vitamin D3-treated and deficient chicks resulted in a differential solubilization of leucine aminopeptidase, maltase, and sucrase activities (114, 195, and 79%, respectively, of appropriate control levels) but not alkaline phosphatase activity. In comparison, proteolysis of purified membranes exhibited vitamin D3- and 1,25-dihydroxycholecalciferol [1,25(OH)2D3]-dependent differences in release of all four marker hydrolases monitored. Calcium uptake studies revealed that preincubation with papain yielded vesicles with a calcium content that was 125% of corresponding native vesicles, in preparations from vitamin D3-treated, as well as deficient birds. Membrane vesicles prepared from 1,25(OH)2D3-treated chicks initially accumulated calcium to a greater extent than those from rachitic birds, but thereafter exhibited a decline in calcium content to basal levels. Preincubation with papain, however, abolished this loss of calcium. The combined results indicate that vitamin D mediates alterations in brush border protein topography and raise the possibility that this action of the seco-steroid might be involved in calcium absorption. However, if vitamin D-stimulated calcium transport across the brush border is dependent on a protein carrier, the molecular entity is not sensitive to inactivation by papain.
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PMID:Vitamin D-mediated alterations in the topography of intestinal brush border proteins: effect of papain on hydrolase release and calcium uptake. 684 6

Homogenates of the posterior latissimus dorsi muscle, a phasic muscle, were fractionated by a one-step zonal centrifugation technique into four major organelle populations and cytoplasmic constituents. These were: (1) Plasma membrane fragments with a modal equilibrium density of 1.10 and containing 5'-nucleotidase, alkaline phosphodiesterase, p-nitrophenylphosphatase and acid phosphatase (beta-glycerophosphate was used as the substrate). (2) Sarcoplasmic reticular fragments which could be further subdivided into calcium transport vesicles, with a model equilibrium density of 1.16, that exhibited calcium uptake; K+-ATPase; leucyl-bet-naphthylamidase; acid phosphodiesterase; acid phosphatase (using cytidine monophosphate as the substrate); and sarcoplasmic reticular lysosomes, with a model equilibrium density of 1.18, possessing dipeptidyl-aminopeptidase II, cathepsin D, alpha-glucosidase, N-acetyl-beta-glucosaminidase, and NADH oxidase activity. (3) Mitochondria with a modal equilibrium density of 1.21. (4) Catalase-containing vesicles with a modal equilibrium density of 1.22; and cytoplasmic constituents (modal density of 1.25) with phosphorylase, pyruvate kinase, myosin-ATPase, aldolase, and protein and RNA content. The purity of these organelles was equal to or better than previous efforts, with a 30-fold purification achieved for 5'-nucleotidase and alkaline phosphodiesterase. These results lend support to the hypothesis that the sarcoplasmic reticulum of phasic muscle, in addition to its specialized role in excitation-contraction coupling, represents a multifunctional membrane system, and that, similar to the smooth endoplasmic reticulum of other cells, it includes some membrane-bound lysosomal enzymes and NADH oxidase.
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PMID:Isopycnic-zonal centrifugation of plasma membrane, sarcoplasmic reticular fragments, lysosomes, and cytoplasmic proteins from phasic skeletal muscle. 721 87


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