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Biosynthesis of intestinal microvillar proteins. Processing of aminopeptidase N by microsomal membranes

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Biosynthesis of intestinal microvillar proteins. Processing of aminopeptidase N by microsomal membranes. / Danielsen, E M; Norén, Ove; Sjöström, H.

I: Biochemical Journal, Bind 212, Nr. 1, 1983, s. 161-5.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Danielsen, EM, Norén, O & Sjöström, H 1983, 'Biosynthesis of intestinal microvillar proteins. Processing of aminopeptidase N by microsomal membranes', Biochemical Journal, bind 212, nr. 1, s. 161-5.

APA

Danielsen, E. M., Norén, O., & Sjöström, H. (1983). Biosynthesis of intestinal microvillar proteins. Processing of aminopeptidase N by microsomal membranes. Biochemical Journal, 212(1), 161-5.

Vancouver

Danielsen EM, Norén O, Sjöström H. Biosynthesis of intestinal microvillar proteins. Processing of aminopeptidase N by microsomal membranes. Biochemical Journal. 1983;212(1):161-5.

Author

Danielsen, E M ; Norén, Ove ; Sjöström, H. / Biosynthesis of intestinal microvillar proteins. Processing of aminopeptidase N by microsomal membranes. I: Biochemical Journal. 1983 ; Bind 212, Nr. 1. s. 161-5.

Bibtex

@article{45f50170e7be11ddbf70000ea68e967b,
title = "Biosynthesis of intestinal microvillar proteins. Processing of aminopeptidase N by microsomal membranes",
abstract = "The biosynthesis of small-intestinal aminopeptidase N (EC 3.4.11.2) was studied in a cell-free translation system derived from rabbit reticulocytes. When dog pancreatic microsomal fractions were present during translation, most of the aminopeptidase N synthesized was found in a membrane-bound rather than a soluble form, indicating that synthesis of the enzyme takes place on ribosomes attached to the rough endoplasmic reticulum. The microsomal fractions process the Mr-115 000 polypeptide, which is the primary translation product of aminopeptidase N, to a polypeptide of Mr 140 000. This was found to be sensitive to the action of endo-beta-N-acetylglucosaminidase H (EC 3.2.1.96), showing that aminopeptidase N undergoes transmembrane glycosylation during synthesis. The position of the signal sequence in aminopeptidase N was determined by a synchronized translation experiment. It was found that microsomal fractions should be added before about 25% of the polypeptide was synthesized to ensure processing to the high-mannose glycosylated form. This suggests that the signal sequence is situated in the N-terminal part of the aminopeptidase N. The size of the cell-free translation product in the absence of microsomal fractions was found to be similar to that on one of the forms of the enzyme obtained from tunicamycin-treated organ-cultured intestinal explants.",
author = "Danielsen, {E M} and Ove Nor{\'e}n and H Sj{\"o}str{\"o}m",
note = "Keywords: Acetylglucosaminidase; Aminopeptidases; Animals; Antigens, CD13; Cell-Free System; Dogs; Intestine, Small; Intracellular Membranes; Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; Membrane Proteins; Microsomes; Microvilli; Organ Culture Techniques; Peptides; Protein Biosynthesis; Swine",
year = "1983",
language = "English",
volume = "212",
pages = "161--5",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "1",

}

RIS

TY - JOUR

T1 - Biosynthesis of intestinal microvillar proteins. Processing of aminopeptidase N by microsomal membranes

AU - Danielsen, E M

AU - Norén, Ove

AU - Sjöström, H

N1 - Keywords: Acetylglucosaminidase; Aminopeptidases; Animals; Antigens, CD13; Cell-Free System; Dogs; Intestine, Small; Intracellular Membranes; Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; Membrane Proteins; Microsomes; Microvilli; Organ Culture Techniques; Peptides; Protein Biosynthesis; Swine

PY - 1983

Y1 - 1983

N2 - The biosynthesis of small-intestinal aminopeptidase N (EC 3.4.11.2) was studied in a cell-free translation system derived from rabbit reticulocytes. When dog pancreatic microsomal fractions were present during translation, most of the aminopeptidase N synthesized was found in a membrane-bound rather than a soluble form, indicating that synthesis of the enzyme takes place on ribosomes attached to the rough endoplasmic reticulum. The microsomal fractions process the Mr-115 000 polypeptide, which is the primary translation product of aminopeptidase N, to a polypeptide of Mr 140 000. This was found to be sensitive to the action of endo-beta-N-acetylglucosaminidase H (EC 3.2.1.96), showing that aminopeptidase N undergoes transmembrane glycosylation during synthesis. The position of the signal sequence in aminopeptidase N was determined by a synchronized translation experiment. It was found that microsomal fractions should be added before about 25% of the polypeptide was synthesized to ensure processing to the high-mannose glycosylated form. This suggests that the signal sequence is situated in the N-terminal part of the aminopeptidase N. The size of the cell-free translation product in the absence of microsomal fractions was found to be similar to that on one of the forms of the enzyme obtained from tunicamycin-treated organ-cultured intestinal explants.

AB - The biosynthesis of small-intestinal aminopeptidase N (EC 3.4.11.2) was studied in a cell-free translation system derived from rabbit reticulocytes. When dog pancreatic microsomal fractions were present during translation, most of the aminopeptidase N synthesized was found in a membrane-bound rather than a soluble form, indicating that synthesis of the enzyme takes place on ribosomes attached to the rough endoplasmic reticulum. The microsomal fractions process the Mr-115 000 polypeptide, which is the primary translation product of aminopeptidase N, to a polypeptide of Mr 140 000. This was found to be sensitive to the action of endo-beta-N-acetylglucosaminidase H (EC 3.2.1.96), showing that aminopeptidase N undergoes transmembrane glycosylation during synthesis. The position of the signal sequence in aminopeptidase N was determined by a synchronized translation experiment. It was found that microsomal fractions should be added before about 25% of the polypeptide was synthesized to ensure processing to the high-mannose glycosylated form. This suggests that the signal sequence is situated in the N-terminal part of the aminopeptidase N. The size of the cell-free translation product in the absence of microsomal fractions was found to be similar to that on one of the forms of the enzyme obtained from tunicamycin-treated organ-cultured intestinal explants.

M3 - Journal article

C2 - 6135417

VL - 212

SP - 161

EP - 165

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 1

ER -

ID: 9881358