@article{793785e0e7bd11ddbf70000ea68e967b,
title = "Enzymatic activity of {"}high-mannose{"} glycosylated forms of intestinal microvillar hydrolases",
abstract = "The {"}high-mannose{"} glycosylated forms of aminopeptidase N (EC 3.4.11.2), maltase-glucoamylase (EC 3.2.1.20), and sucrase-isomaltase (EC 3.2.1.48, EC 3.2.1.10) have been purified. The high-mannose glycosylated form of sucrase-isomaltase was found to have a lower specific activity than the complex glycosylated form, whereas no difference was observed for the two other enzymes. The change in glycosylation from high-mannose to complex form thus seems to be of importance for the enzymatic activity of sucrase-isomaltase either by direct structural involvement or by a general stabilization effect on the protein conformation.",
author = "H Sj{\"o}str{\"o}m and Ove Nor{\'e}n and Danielsen, {E M}",
note = "Keywords: Aminopeptidases; Animals; Antigens, CD13; Glucosidases; Intestinal Mucosa; Mannose; Microvilli; Multienzyme Complexes; Sucrase-Isomaltase Complex; Swine; alpha-Glucosidases",
year = "1985",
language = "English",
volume = "4",
pages = "980--3",
journal = "Journal of Pediatric Gastroenterology and Nutrition",
issn = "0277-2116",
publisher = "Lippincott Williams & Wilkins",
number = "6",
}