Luminal Starch Substrate “Brake” on Maltase-Glucoamylase Activity Is Located within the Glucoamylase Subunit
نویسندگان
چکیده
منابع مشابه
Direct starch digestion by sucrase-isomaltase and maltase-glucoamylase.
1. Jane J, Chen YY, Lee LF, et al. Effects of amylopectin branch chain length and amylose content on the gelatinization and pasting properties of starch. Cereal Chem 1999;76:629–37. 2. Quezada-Calvillo R, Robayo-Torres CC, Opekum AR, et al. Contribution of mucosal maltase-glucoamylase activities to mouse small intestinal starch alpha-glucogenesis. J Nutr 2007;137:1725–33. 3. Nichols BL, Quezada...
متن کاملNeutral maltase/glucoamylase from rabbit renal cortex.
Maltase activity (EC 3.2.1.20) was solubilized from rabbit kidney brush-border membrane by using 1.0% Triton X-100 and purified 230-fold with an overall recovery of 30%. The purification procedure makes use of heat precipitation, chromatography on DE-52 DEAE-cellulose and gel filtration on Sephacryl S-300. Rabbit kidney brush border exhibited glucoamylase activity with a maltase/glucoamylase ra...
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One of the most important carbohydrate-splitting enzymes is themaltase-glucoamylase which catalyzes the hydrolysis of alpha-glucosidic linkages. Maltase-glucoamylase inhibitors during the last few years have aroused medical interests in the treatment of diabetes. They contribute to a better understanding of the mechanism of maltase-glucoamylase. At present there are many different classes of ma...
متن کاملClinical aspects and treatment of congenital sucrase-isomaltase deficiency.
30. Chantret I, Lacasa M, Chevalier G, et al. Sequence of the complete cDNA and the 50 structure of the human sucrase-isomaltase gene. Possible homology with a yeast glucoamylase. Biochem J 1992; 285:915–23. 31. Nichols BL, Eldering J, Avery S, et al. Human small intestinal maltaseglucoamylase cDNA cloning. Homology to sucrase-isomaltase. J Biol Chem 1998;273:3076–81. 32. Nichols BL, Avery S, S...
متن کاملIsolation of a detergent-solubilized maltase/glucoamylase from rat intestine and its comparison with a maltase/glucoamylase solubilized by papain.
Maltase/glucoamylase from the rat intestinal brush-border membrane was solubilized by homogenization of the intestinal mucosa in buffer containing 0.5% Triton X-100. After removal of the detergent with butan-1-ol, the enzyme was purified by chromatography on Sepharose 4B and DEAE-cellulose. The final specific activity was 70.3 units/mg of protein in six preparations, comparing favourably with t...
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ژورنال
عنوان ژورنال: The Journal of Nutrition
سال: 2008
ISSN: 0022-3166,1541-6100
DOI: 10.1093/jn/138.4.685