Abstract
Immunoglobulins have been identified as membrane-bound molecules on the surface of B lymphocytes and as secreted products of plasma cells. In the case of immunoglobulin M(IgM) the carboxy-terminal sequences of the μ-chains of membrane-bound and secreted molecules differ from each other and are encoded by different exons of the μ constant region (Cμ) gene. The coding sequence for the C-terminus of the secreted μ-chain is contiguous with the 3′ end of the Cμ4 exon and separate exons downstream of Cμ4 encode the C-terminus of the membrane-bound chain1–3. Immunoglobulin D is also found membrane-bound and as a secreted molecule, and recent data indicate that the exon arrangement of the Cδ gene is in part similar to that of the Cμ gene4,5. However, the amino acid sequence analysis presented here demonstrates that in the case of IgD the C-terminus of the secreted δ-chain is encoded by a separate exon (the CδDC exon of Tucker et al.5) and not by the CδAC sequence which corresponds topographically to the sequence expressed at the C-terminus of secreted μ chains.
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Dildrop, R., Beyreuther, K. C-terminal sequence of the secreted form of mouse IgD heavy chain. Nature 292, 61–63 (1981). https://doi.org/10.1038/292061a0
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DOI: https://doi.org/10.1038/292061a0
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