Luminal Substrate “Brake” on Mucosal Maltase-glucoamylase Activity Regulates Total Rate of Starch Digestion to Glucose-Reference-Cited by-同舟云学术

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Luminal Substrate “Brake” on Mucosal Maltase-glucoamylase Activity Regulates Total Rate of Starch Digestion to Glucose

Published:2007-07 Issue:1 Volume:45 Page:32-43
ISSN:0277-2116
Container-title:Journal of Pediatric Gastroenterology & Nutrition
language:en
Short-container-title:

Author:

Quezada-Calvillo Roberto,Robayo-Torres Claudia C,Ao Zihua,Hamaker Bruce R,Quaroni Andrea,Brayer Gary D,Sterchi Erwin E,Baker Susan S,Nichols Buford L

Publisher

Ovid Technologies (Wolters Kluwer Health)

Subject

Gastroenterology,Pediatrics, Perinatology, and Child Health

Reference47 articles.

1. Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques;Brayer;Biochemistry,2000

2. Column chromatography of human small-intestinal maltase, isomaltase and invertase activities;Dahlqvist;Biochem J,1969

3. The hydrolysis of the naturally occurring alpha-glucosides by the human intestinal mucosa;Eggermont;Eur J Biochem,1969

4. Di- and oligosaccharide substrate specificities and subsite binding energies of pig intestinal glucoamylase-maltase;Gunther;Arch Biochem Biophys,1998

5. Acarbose and 1-deoxynojirimycin inhibit maltose and maltooligosaccharide hydrolysis of human small intestinal glucoamylase-maltase in two different substrate-induced modes;Breitmeier;Arch Biochem Biophys,1997

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