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XB-ART-28474
FEBS Lett 1986 Nov 24;2082:369-72.
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Synthesis, processing, and secretion of rat immunoglobulin E made in Xenopus oocytes.

Lund T , Bravo R , Johansen HR , Zeuthen J , Vuust J .


Abstract
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 (e-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.

PubMed ID: 3780973
Article link: FEBS Lett