Abstract
Biosynthetic studies in the presence of an inhibitor of glycosylation indicate that individual human lymphoma-derived cell lines can synthesize both membrane receptor and presumptive secretory forms of IgM μ chains. The receptor form has a larger polypeptide chain than the secretory form and possesses a different C-terminus, but similar N-terminus, consistent with the presence of a C-terminal hydrophobic ‘tail’ for integral membrane binding. Messenger RNA isolated from these cells directs the synthesis of both forms of μ chain in a wheat germ translation system, indicating the presence of independent mRNAs for each form. It is proposed that the synthetic pathways for receptor and secretory IgM diverge at the post-transcriptional level, possibly by differential RNA splicing to give mRNA molecules with or without a translatable ‘tail’ segment.
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Singer, P., Singer, H. & Williamson, A. Different species of messenger RNA encode receptor and secretory IgM μ chains differing at their carboxy termini. Nature 285, 294–300 (1980). https://doi.org/10.1038/285294a0
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DOI: https://doi.org/10.1038/285294a0
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