Biosynthesis of intestinal microvillar proteins. Translational evidence in vitro that aminopeptidase N is synthesized as a Mr-115000 polypeptide

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Standard

Biosynthesis of intestinal microvillar proteins. Translational evidence in vitro that aminopeptidase N is synthesized as a Mr-115000 polypeptide. / Danielsen, Erik Michael; Norén, O; Sjöström, H.

In: Biochemical Journal, Vol. 204, No. 1, 1982, p. 323-7.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Danielsen, EM, Norén, O & Sjöström, H 1982, 'Biosynthesis of intestinal microvillar proteins. Translational evidence in vitro that aminopeptidase N is synthesized as a Mr-115000 polypeptide', Biochemical Journal, vol. 204, no. 1, pp. 323-7.

APA

Danielsen, E. M., Norén, O., & Sjöström, H. (1982). Biosynthesis of intestinal microvillar proteins. Translational evidence in vitro that aminopeptidase N is synthesized as a Mr-115000 polypeptide. Biochemical Journal, 204(1), 323-7.

Vancouver

Danielsen EM, Norén O, Sjöström H. Biosynthesis of intestinal microvillar proteins. Translational evidence in vitro that aminopeptidase N is synthesized as a Mr-115000 polypeptide. Biochemical Journal. 1982;204(1):323-7.

Author

Danielsen, Erik Michael ; Norén, O ; Sjöström, H. / Biosynthesis of intestinal microvillar proteins. Translational evidence in vitro that aminopeptidase N is synthesized as a Mr-115000 polypeptide. In: Biochemical Journal. 1982 ; Vol. 204, No. 1. pp. 323-7.

Bibtex

@article{d0040d706c7a11de8bc9000ea68e967b,
title = "Biosynthesis of intestinal microvillar proteins. Translational evidence in vitro that aminopeptidase N is synthesized as a Mr-115000 polypeptide",
abstract = "A crude RNA fraction, prepared from pig small intestine, was found to be more efficient than a fraction enriched in polyadenylated RNA in directing translation of polypeptides with Mr greater than 100000 in a rabbit reticulocyte lysate system. Aminopeptidase N (EC 3.4.11.2) synthesized in vitro was immunopurified from the translation mixture and analysed by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. It was found to have an apparent Mr of 115000 regardless of whether the translation was performed in the absence or presence of proteinase inhibitors. This result contradicts the possibility of aminopeptidase N being synthesized as a large single-chain precursor polypeptide.",
author = "Danielsen, {Erik Michael} and O Nor{\'e}n and H Sj{\"o}str{\"o}m",
note = "Keywords: Aminopeptidases; Animals; Antigens, CD13; Electrophoresis, Polyacrylamide Gel; Enzyme Precursors; Intestine, Small; Macromolecular Substances; Microvilli; Peptide Biosynthesis; Protein Biosynthesis; RNA; Swine",
year = "1982",
language = "English",
volume = "204",
pages = "323--7",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "1",

}

RIS

TY - JOUR

T1 - Biosynthesis of intestinal microvillar proteins. Translational evidence in vitro that aminopeptidase N is synthesized as a Mr-115000 polypeptide

AU - Danielsen, Erik Michael

AU - Norén, O

AU - Sjöström, H

N1 - Keywords: Aminopeptidases; Animals; Antigens, CD13; Electrophoresis, Polyacrylamide Gel; Enzyme Precursors; Intestine, Small; Macromolecular Substances; Microvilli; Peptide Biosynthesis; Protein Biosynthesis; RNA; Swine

PY - 1982

Y1 - 1982

N2 - A crude RNA fraction, prepared from pig small intestine, was found to be more efficient than a fraction enriched in polyadenylated RNA in directing translation of polypeptides with Mr greater than 100000 in a rabbit reticulocyte lysate system. Aminopeptidase N (EC 3.4.11.2) synthesized in vitro was immunopurified from the translation mixture and analysed by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. It was found to have an apparent Mr of 115000 regardless of whether the translation was performed in the absence or presence of proteinase inhibitors. This result contradicts the possibility of aminopeptidase N being synthesized as a large single-chain precursor polypeptide.

AB - A crude RNA fraction, prepared from pig small intestine, was found to be more efficient than a fraction enriched in polyadenylated RNA in directing translation of polypeptides with Mr greater than 100000 in a rabbit reticulocyte lysate system. Aminopeptidase N (EC 3.4.11.2) synthesized in vitro was immunopurified from the translation mixture and analysed by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. It was found to have an apparent Mr of 115000 regardless of whether the translation was performed in the absence or presence of proteinase inhibitors. This result contradicts the possibility of aminopeptidase N being synthesized as a large single-chain precursor polypeptide.

M3 - Journal article

C2 - 6180737

VL - 204

SP - 323

EP - 327

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 1

ER -

ID: 13063652