Synthesis of surface immunoglobulin E receptor in Xenopus oocytes by translation of mRNA from rat basophilic leukemia cells

Fu-Tong Liu, N. Orida

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Immunoglobulin E-binding activity was expressed in Xenopus oocytes injected with mRNA from rat basophilic leukemia cells which possess abundant immunoglobulin E (IgE) receptor. Such activity was demonstrated with intact oocytes by their binding of 125I-labeled mouse monoclonal IgE. Binding activity was specific as shown by the total inhibition of 125I-IgE binding by unlabeled IgE but not by unlabeled IgG1. The relevance of the IgE-binding activity to the IgE receptor was also supported by the absence of this activity in oocytes injected with mRNA from cells lacking surface IgE receptors. mRNA coding from the IgE-binding activity was enriched in fractions sedimenting at 13.5 S in sucrose density gradients. From oocytes injected with rat basophilic leukemia mRNA, two major polypeptides were isolated by affinity purification on IgE immunoadsorbent. One [M(r) = 31,000] is equivalent in size to the previously identified 'receptor-associated protein'; the other [M(r) = 40,000] is speculated to be a partially glycosylated or unglycosylated form of the α subunit of the IgE receptor. The binding of IgE-coated fluorescent microspheres by oocytes injected with rat basophilic leukemia mRNA demonstrated the surface expression of the IgE-binding proteins.

Original languageEnglish (US)
Pages (from-to)10649-10652
Number of pages4
JournalJournal of Biological Chemistry
Volume259
Issue number17
StatePublished - 1984

Fingerprint

IgE Receptors
B-Cell Antigen Receptors
Protein Biosynthesis
Xenopus
Immunoglobulin E
Oocytes
Rats
Leukemia
Messenger RNA
Immunosorbents
Microspheres
Purification
Sucrose
Carrier Proteins
Immunoglobulin G
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Synthesis of surface immunoglobulin E receptor in Xenopus oocytes by translation of mRNA from rat basophilic leukemia cells. / Liu, Fu-Tong; Orida, N.

In: Journal of Biological Chemistry, Vol. 259, No. 17, 1984, p. 10649-10652.

Research output: Contribution to journalArticle

@article{026c1f3b702645aab7cafca7770365fe,
title = "Synthesis of surface immunoglobulin E receptor in Xenopus oocytes by translation of mRNA from rat basophilic leukemia cells",
abstract = "Immunoglobulin E-binding activity was expressed in Xenopus oocytes injected with mRNA from rat basophilic leukemia cells which possess abundant immunoglobulin E (IgE) receptor. Such activity was demonstrated with intact oocytes by their binding of 125I-labeled mouse monoclonal IgE. Binding activity was specific as shown by the total inhibition of 125I-IgE binding by unlabeled IgE but not by unlabeled IgG1. The relevance of the IgE-binding activity to the IgE receptor was also supported by the absence of this activity in oocytes injected with mRNA from cells lacking surface IgE receptors. mRNA coding from the IgE-binding activity was enriched in fractions sedimenting at 13.5 S in sucrose density gradients. From oocytes injected with rat basophilic leukemia mRNA, two major polypeptides were isolated by affinity purification on IgE immunoadsorbent. One [M(r) = 31,000] is equivalent in size to the previously identified 'receptor-associated protein'; the other [M(r) = 40,000] is speculated to be a partially glycosylated or unglycosylated form of the α subunit of the IgE receptor. The binding of IgE-coated fluorescent microspheres by oocytes injected with rat basophilic leukemia mRNA demonstrated the surface expression of the IgE-binding proteins.",
author = "Fu-Tong Liu and N. Orida",
year = "1984",
language = "English (US)",
volume = "259",
pages = "10649--10652",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "17",

}

TY - JOUR

T1 - Synthesis of surface immunoglobulin E receptor in Xenopus oocytes by translation of mRNA from rat basophilic leukemia cells

AU - Liu, Fu-Tong

AU - Orida, N.

PY - 1984

Y1 - 1984

N2 - Immunoglobulin E-binding activity was expressed in Xenopus oocytes injected with mRNA from rat basophilic leukemia cells which possess abundant immunoglobulin E (IgE) receptor. Such activity was demonstrated with intact oocytes by their binding of 125I-labeled mouse monoclonal IgE. Binding activity was specific as shown by the total inhibition of 125I-IgE binding by unlabeled IgE but not by unlabeled IgG1. The relevance of the IgE-binding activity to the IgE receptor was also supported by the absence of this activity in oocytes injected with mRNA from cells lacking surface IgE receptors. mRNA coding from the IgE-binding activity was enriched in fractions sedimenting at 13.5 S in sucrose density gradients. From oocytes injected with rat basophilic leukemia mRNA, two major polypeptides were isolated by affinity purification on IgE immunoadsorbent. One [M(r) = 31,000] is equivalent in size to the previously identified 'receptor-associated protein'; the other [M(r) = 40,000] is speculated to be a partially glycosylated or unglycosylated form of the α subunit of the IgE receptor. The binding of IgE-coated fluorescent microspheres by oocytes injected with rat basophilic leukemia mRNA demonstrated the surface expression of the IgE-binding proteins.

AB - Immunoglobulin E-binding activity was expressed in Xenopus oocytes injected with mRNA from rat basophilic leukemia cells which possess abundant immunoglobulin E (IgE) receptor. Such activity was demonstrated with intact oocytes by their binding of 125I-labeled mouse monoclonal IgE. Binding activity was specific as shown by the total inhibition of 125I-IgE binding by unlabeled IgE but not by unlabeled IgG1. The relevance of the IgE-binding activity to the IgE receptor was also supported by the absence of this activity in oocytes injected with mRNA from cells lacking surface IgE receptors. mRNA coding from the IgE-binding activity was enriched in fractions sedimenting at 13.5 S in sucrose density gradients. From oocytes injected with rat basophilic leukemia mRNA, two major polypeptides were isolated by affinity purification on IgE immunoadsorbent. One [M(r) = 31,000] is equivalent in size to the previously identified 'receptor-associated protein'; the other [M(r) = 40,000] is speculated to be a partially glycosylated or unglycosylated form of the α subunit of the IgE receptor. The binding of IgE-coated fluorescent microspheres by oocytes injected with rat basophilic leukemia mRNA demonstrated the surface expression of the IgE-binding proteins.

UR - http://www.scopus.com/inward/record.url?scp=0021193423&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021193423&partnerID=8YFLogxK

M3 - Article

VL - 259

SP - 10649

EP - 10652

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 17

ER -