In vitro translation of intestinal sucrase-isomaltase and glucoamylase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference16 articles.
1. A fully active, two-active-site, single-chain sucrase.isomaltase from pig small intestine. Implications for the biosynthesis of a mammalian integral stalked membrane protein.
2. Amphiphilic Pig Intestinal Microvillus Maltase/Glucoamylase. Structure and Specificity
3. Mapping of proteolytic and cyanogen bromide peptides from subunits of intestinal maltase–glucoamylase: evidence for significant homology
4. The primary translation product of rat intestinal apolipoprotein A-I mRNA is an unusual preproprotein.
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1. Starch Digestion and Patients With Congenital Sucrase-Isomaltase Deficiency;Journal of Pediatric Gastroenterology & Nutrition;2012-11
2. Comparative expression of hexose transporters (SGLT1, GLUT1, GLUT2 and GLUT5) throughout the mouse gastrointestinal tract;Histochemistry and Cell Biology;2011-01-28
3. Structural changes and inhibition of sucrase after binding of scopolamine;European Journal of Pharmacology;2010-06
4. Sucrase-isomaltase is an adenosine 3',5'-cyclic monophosphate–dependent epithelial chloride channel;Gastroenterology;2001-01
5. Determinants of regional sucrase-isomaltase expression in adult rat small intestine.;Journal of Biological Chemistry;1991-11
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