Enzymatic activity of "high-mannose" glycosylated forms of intestinal microvillar hydrolases
Research output: Contribution to journal › Journal article › Research › peer-review
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 language | English |
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Journal | Journal of Pediatric Gastroenterology and Nutrition |
Volume | 4 |
Issue number | 6 |
Pages (from-to) | 980-3 |
Number of pages | 3 |
ISSN | 0277-2116 |
Publication status | Published - 1985 |
Bibliographical note
Keywords: Aminopeptidases; Animals; Antigens, CD13; Glucosidases; Intestinal Mucosa; Mannose; Microvilli; Multienzyme Complexes; Sucrase-Isomaltase Complex; Swine; alpha-Glucosidases
ID: 9881247