Biosynthesis of intestinal microvillar proteins. Effect of castanospermine on cell-free synthesis of aminopeptidase N.

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Standard

Biosynthesis of intestinal microvillar proteins. Effect of castanospermine on cell-free synthesis of aminopeptidase N. / Danielsen, E M; Olsen, Jørgen.

In: FEBS Letters, Vol. 228, No. 1, 1988, p. 102-4.

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

Harvard

Danielsen, EM & Olsen, J 1988, 'Biosynthesis of intestinal microvillar proteins. Effect of castanospermine on cell-free synthesis of aminopeptidase N.', FEBS Letters, vol. 228, no. 1, pp. 102-4.

APA

Danielsen, E. M., & Olsen, J. (1988). Biosynthesis of intestinal microvillar proteins. Effect of castanospermine on cell-free synthesis of aminopeptidase N. FEBS Letters, 228(1), 102-4.

Vancouver

Danielsen EM, Olsen J. Biosynthesis of intestinal microvillar proteins. Effect of castanospermine on cell-free synthesis of aminopeptidase N. FEBS Letters. 1988;228(1):102-4.

Author

Danielsen, E M ; Olsen, Jørgen. / Biosynthesis of intestinal microvillar proteins. Effect of castanospermine on cell-free synthesis of aminopeptidase N. In: FEBS Letters. 1988 ; Vol. 228, No. 1. pp. 102-4.

Bibtex

@article{9661abc099fa11dd86a6000ea68e967b,
title = "Biosynthesis of intestinal microvillar proteins. Effect of castanospermine on cell-free synthesis of aminopeptidase N.",
abstract = "Pig small intestinal mRNA was translated in a rabbit reticulocyte lysate system supplemented with microsomal membranes. Castanospermine, an inhibitor of glucosidase I, induced a high mannose-glycosylated form of microvillar aminopeptidase N (EC 3.4.11.2) of increased molecular mass, indicating the blocked removal of glucose residues. In contrast to its reduced expression in a mucosal explant system [(1986) Biochem. J. 240, 777-782], this molecular form of aminopeptidase N was at least as abundant in cell-free translation as its normal high mannose-glycosylated counterpart, ruling out degradation taking place in the rough endoplasmic reticulum. Degradation of newly produced, malprocessed enzyme must therefore occur at a later stage during intracellular transport, presumably in the sarcoplasmic reticulum or in transitional elements between this organelle and the Golgi complex.",
author = "Danielsen, {E M} and J{\o}rgen Olsen",
note = "Keywords: Alkaloids; Aminopeptidases; Animals; Antigens, CD13; Binding Sites; Cell-Free System; Indolizines; Intestine, Small; Microvilli; RNA, Messenger; Swine",
year = "1988",
language = "English",
volume = "228",
pages = "102--4",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "1",

}

RIS

TY - JOUR

T1 - Biosynthesis of intestinal microvillar proteins. Effect of castanospermine on cell-free synthesis of aminopeptidase N.

AU - Danielsen, E M

AU - Olsen, Jørgen

N1 - Keywords: Alkaloids; Aminopeptidases; Animals; Antigens, CD13; Binding Sites; Cell-Free System; Indolizines; Intestine, Small; Microvilli; RNA, Messenger; Swine

PY - 1988

Y1 - 1988

N2 - Pig small intestinal mRNA was translated in a rabbit reticulocyte lysate system supplemented with microsomal membranes. Castanospermine, an inhibitor of glucosidase I, induced a high mannose-glycosylated form of microvillar aminopeptidase N (EC 3.4.11.2) of increased molecular mass, indicating the blocked removal of glucose residues. In contrast to its reduced expression in a mucosal explant system [(1986) Biochem. J. 240, 777-782], this molecular form of aminopeptidase N was at least as abundant in cell-free translation as its normal high mannose-glycosylated counterpart, ruling out degradation taking place in the rough endoplasmic reticulum. Degradation of newly produced, malprocessed enzyme must therefore occur at a later stage during intracellular transport, presumably in the sarcoplasmic reticulum or in transitional elements between this organelle and the Golgi complex.

AB - Pig small intestinal mRNA was translated in a rabbit reticulocyte lysate system supplemented with microsomal membranes. Castanospermine, an inhibitor of glucosidase I, induced a high mannose-glycosylated form of microvillar aminopeptidase N (EC 3.4.11.2) of increased molecular mass, indicating the blocked removal of glucose residues. In contrast to its reduced expression in a mucosal explant system [(1986) Biochem. J. 240, 777-782], this molecular form of aminopeptidase N was at least as abundant in cell-free translation as its normal high mannose-glycosylated counterpart, ruling out degradation taking place in the rough endoplasmic reticulum. Degradation of newly produced, malprocessed enzyme must therefore occur at a later stage during intracellular transport, presumably in the sarcoplasmic reticulum or in transitional elements between this organelle and the Golgi complex.

M3 - Journal article

C2 - 2893745

VL - 228

SP - 102

EP - 104

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 1

ER -

ID: 6586557