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