Synthesis, processing, and secretion of rat immunoglobulin E made in Xenopus oocytes.
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.
D000818:Animals; D006031:Glycosylation; D007073:Immunoglobulin E / Q000096:biosynthesis* / Q000378:metabolism; D008845:Microinjections; D008970:Molecular Weight; D009865:Oocytes / Q000378:metabolism; D014176:Protein Biosynthesis; D011499:Protein Processing, Post-Translational; D012333:RNA, Messenger / Q000235:genetics; D051381:Rats; D014982:Xenopus laevis
D012333:RNA, Messenger; D007073:Immunoglobulin E