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 substrate specificity of honeybee alpha-glucosidase I, a monomeric enzyme was kinetically investigated. Unusual kinetic features were observed in the cleavage reactions of sucrose, maltose, p-nitrophenyl alpha-glucoside, phenyl alpha-glucoside, turanose, and maltodextrin (DP = 13). At relatively high substrate concentrations, the velocities of liberation of fructose from sucrose, glucose from maltose, p-nitrophenol from p-nitrophenyl alpha-glucoside, and phenol from phenyl alpha-glucoside were accelerated, and so the Lineweaver-Burk plots were convex, indicating negative kinetic cooperativity: the Hill coefficients were calculated to be 0.50, 0.64, 0.50, and 0.67 for sucrose, maltose, p-nitrophenyl alpha-glucoside, and phenyl alpha-glucoside, respectively. For the degradation of turanose and maltodextrin, the enzyme showed a sigmoidal curve in v versus s plots and thus catalyzed the reaction with positive kinetic cooperativity. The Lineweaver-Burk plots were concave and the Hill coefficients were 1.2 and 1.5 for turanose and maltodextrin, respectively. These unique properties cannot be interpreted by the reaction mechanism that Huber and Thompson proposed: (1973) Biochemistry 12, 4011-4020. The rate parameters for the hydrolysis of sucrose, maltose, p-nitrophenyl alpha-glucoside and phenyl alpha-glucoside were estimated by extrapolating the linear part of the Lineweaver-Burk plots at low substrate concentrations.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Allosteric properties, substrate specificity, and subsite affinities of honeybee alpha-glucosidase I. 220 17

A model of nonischemic hypoxia of the jejunum was designed in dogs, by shunting of blood from the inferior vena cava directly into the regional mesenteric arterial supply, thereby lowering the PaO2 of the blood that reached the jejunal wall from 98.6 +/- 3 to 62 +/- 5 mm Hg. Absorption rates of sodium, glucose, fructose, glycine, and the dibasic aminoacid lysine were studied by in situ luminal perfusion of a 30-cm proximal jejunal segment with a bicarbonate buffer solution containing phenol red as a nonabsorbable marker for determination of water fluxes. During periods of control, hypoxia, and after discontinuation of the venoarterial admixture (recovery), effluent perfusate was collected and mucosal biopsies were obtained for assay of lactase, maltase and sucrase activity, mucosal ATPase activity and ATP content, and for light- and electron microscopic examination. Mesenteric supply with hypoxic blood was associated with a significant inhibition of Na+,K+-ATPase activity (p less than 0.001) and a rise in mucosal ATP content (p less than 0.05). There was a significant reduction in the absorption rates of sodium (p less than 0.001), glucose, and glycine (p less than 0.01), but no change in the transport of fructose and of lysine. Brush border enzymes were unaltered. The histological appearance of the mucosa remained normal throughout the experiment, but on electron microscopy a distinct swelling of the enterocyte mitochondria was noted during the hypoxia period.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effects of nonischemic hypoxia on jejunal mucosal structure and function: study of an experimental model in dogs. 294 46

The gastric emptying of sucrose and maltose solutions at different concentrations, with addition of phenol red (6 mg%) used as a marker, was studied in 144 Wistar male rats. The gastric retention was determined 15 minutes after the orogastric infusion of sucrose and maltose solutions at 2.5%, 5% and 10% and volume of 1 and 2 ml/100 g weight of the animal, making 1 use of 12 rats for each volume and concentration. The activities of lactase, sucrase and maltase were evaluated in other eight rat's small intestine. The results demonstrated a maltase/sucrase activity rate of 4:1. The gastric retentions of the maltose solution were significantly higher than sucrose solution at 10% and 5% concentration, either 1 and 2 ml/100 g weight. There were no differences between gastric retention at 2.5% concentration neither with 2 nor 1 ml/100 g weight. As an explanation of these results it is proposed that the faster gastric emptying of sucrose solution 10% and 5% in relation with the same concentrations of maltose is due to a probable saturation of sucrase, that when achieved, interrupts the regulation of gastric emptying, determined by the intestinal receptors.
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PMID:[Gastric emptying of sucrose and maltose and levels of respective disaccharidases in the small intestinal mucosa of adult rats]. 787 66

A novel alpha-glucosidase with an apparent subunit mass of 59 +/- 0. 5 kDa was purified from protein extracts of Rhizobium sp. strain USDA 4280, a nodulating strain of black locust (Robinia pseudoacacia L), and characterized. After purification to homogeneity (475-fold; yield, 18%) by ammonium sulfate precipitation, cation-exchange chromatography, hydrophobic chromatography, dye chromatography, and gel filtration, this enzyme had a pI of 4.75 +/- 0.05. The enzyme activity was optimal at pH 6.0 to 6.5 and 35 degrees C. The activity increased in the presence of NH4+ and K+ ions but was inhibited by Cu2+, Ag+, Hg+, and Fe2+ ions and by various phenyl, phenol, and flavonoid derivatives. Native enzyme activity was revealed by native gel electrophoresis and isoelectrofocusing-polyacrylamide gel electrophoresis with fluorescence detection in which 4-methylumbelliferyl alpha-glucoside was the fluorogenic substrate. The enzyme was more active with alpha-glucosides substituted with aromatic aglycones than with oligosaccharides. This alpha-glucosidase exhibited Michaelis-Menten kinetics with 4-methylumbelliferyl alpha-D-glucopyranoside (Km, 0.141 microM; Vmax, 6.79 micromol min-1 mg-1) and with p-nitrophenyl alpha-D-glucopyranoside (Km, 0.037 microM; Vmax, 2.92 micromol min-1 mg-1). Maltose, trehalose, and sucrose were also hydrolyzed by this enzyme.
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PMID:Purification and characterization of an alpha-glucosidase from Rhizobium sp. (Robinia pseudoacacia L.) strain USDA 4280. 1038 82

The crucial medicinal plant Dalbergia odorifera T. Chen species belongs to genus Dalbergia, with interesting secondary metabolites, consisting of main classes of flavonoid, phenol, and sesquiterpene derivatives, as well as several arylbenzofurans, quinones, and fatty acids. Biological studies were carried out on extracts, fractions, and compounds from this species involved in cytotoxic assays; antibacterial, antioxidative, anti-inflammatory, antithrombotic, antiplatelet, antiosteosarcoma, antiosteoporosis, antiangiogenesis, and prostaglandin biosynthetic enzyme inhibition activities; vasorelaxant activities; alpha-glucosidase inhibitory activities; and many other effects. In terms of the valuable resources for natural new drugs development, D. odorifera species are widely used as medicinal drugs in many countries for treatment of cardiovascular diseases, cancer, diabetes, blood disorders, ischemia, swelling, necrosis, or rheumatic pain. Although natural products from this plant have been increasingly playing an important role in drug discovery programs, there is no supportive evidence to provide a general insight into phytochemical studies on D. odorifera species and biological activities of extracts, fractions, and isolated compounds. To a certain extent, this review deals with an overview of almost naturally occurring compounds from this species, along with extensive coverage of their biological evaluations.
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PMID:A Review on the Medicinal Plant Dalbergia odorifera Species: Phytochemistry and Biological Activity. 2934 71