Enzymatic activity of "high-mannose" glycosylated forms of intestinal microvillar hydrolases

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  • H Sjöström
  • Ove Norén
  • E M Danielsen
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.
Original languageEnglish
JournalJournal of Pediatric Gastroenterology and Nutrition
Volume4
Issue number6
Pages (from-to)980-3
Number of pages3
ISSN0277-2116
Publication statusPublished - 1985

Bibliographical note

Keywords: Aminopeptidases; Animals; Antigens, CD13; Glucosidases; Intestinal Mucosa; Mannose; Microvilli; Multienzyme Complexes; Sucrase-Isomaltase Complex; Swine; alpha-Glucosidases

ID: 9881247