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

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Standard

Enzymatic activity of "high-mannose" glycosylated forms of intestinal microvillar hydrolases. / Sjöström, H; Norén, Ove; Danielsen, E M.

I: Journal of Pediatric Gastroenterology and Nutrition, Bind 4, Nr. 6, 1985, s. 980-3.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Sjöström, H, Norén, O & Danielsen, EM 1985, 'Enzymatic activity of "high-mannose" glycosylated forms of intestinal microvillar hydrolases', Journal of Pediatric Gastroenterology and Nutrition, bind 4, nr. 6, s. 980-3.

APA

Sjöström, H., Norén, O., & Danielsen, E. M. (1985). Enzymatic activity of "high-mannose" glycosylated forms of intestinal microvillar hydrolases. Journal of Pediatric Gastroenterology and Nutrition, 4(6), 980-3.

Vancouver

Sjöström H, Norén O, Danielsen EM. Enzymatic activity of "high-mannose" glycosylated forms of intestinal microvillar hydrolases. Journal of Pediatric Gastroenterology and Nutrition. 1985;4(6):980-3.

Author

Sjöström, H ; Norén, Ove ; Danielsen, E M. / Enzymatic activity of "high-mannose" glycosylated forms of intestinal microvillar hydrolases. I: Journal of Pediatric Gastroenterology and Nutrition. 1985 ; Bind 4, Nr. 6. s. 980-3.

Bibtex

@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",

}

RIS

TY - JOUR

T1 - Enzymatic activity of "high-mannose" glycosylated forms of intestinal microvillar hydrolases

AU - Sjöström, H

AU - Norén, Ove

AU - Danielsen, E M

N1 - Keywords: Aminopeptidases; Animals; Antigens, CD13; Glucosidases; Intestinal Mucosa; Mannose; Microvilli; Multienzyme Complexes; Sucrase-Isomaltase Complex; Swine; alpha-Glucosidases

PY - 1985

Y1 - 1985

N2 - 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.

AB - 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.

M3 - Journal article

C2 - 2866240

VL - 4

SP - 980

EP - 983

JO - Journal of Pediatric Gastroenterology and Nutrition

JF - Journal of Pediatric Gastroenterology and Nutrition

SN - 0277-2116

IS - 6

ER -

ID: 9881247