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Synthesis, processing, and secretion of rat immunoglobulin E made in Xenopus oocytes
Author(s) -
Lund Torben,
Bravo Rodrigo,
Johansen Hanne R.,
Zeuthen Jesper,
Vuust Jens
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81051-1
Subject(s) - xenopus , immunoprecipitation , immunoglobulin e , glycosylation , immunoglobulin heavy chain , antibody , microbiology and biotechnology , immunoglobulin light chain , chemistry , secretion , immunoglobulin d , gel electrophoresis , polyacrylamide gel electrophoresis , messenger rna , biology , biochemistry , immunology , gene , b cell , enzyme
Rat immunoglobulin E (IgE) synthesized in Xenopus laevis oocytes, injected with rat plasmacytoma mRNA, was analysed by specific immunoprecipitation and SDS‐polyacrylamide gel electrophoresis under reducing as well as non‐reducing conditions. The results indicate that the oocytes will translate and correctly process the rat IgE heavy and light chains, resulting in secretion of a correctly assembled, normal immunoglobulin molecule. The normal, extensive glycosylation of the IgE heavy chain (ε‐chain) is faithfully carried out by the oocytes; therefore, this posttranslational modification is apparently of an unspecific nature, and does not depend upon a mechanism specific for plasma cells.