Switch from hapten-specific immunoglobulin M to immunoglobulin D secretion in a hybrid mouse cell line.

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Abstract
From a hybrid mouse [mouse myeloma cell spleen cell] cell line (B1-8) that secreted an IgM,.lambda.1 anti-(4-hydroxy-3-nitrophenyl)acetyl antibody but that had no detectable surface IgM, selection for a variant with .lambda.1 chains on the surface resulted in the isolation of a line that had switched from .mu. to .delta. expression. The surface and secreted Ig of this line were typed as IgD with 2 monoclonal antibodies; the parental IgM and variant IgD molecules carried the same variable regions as judged by hapten-binding and idiotypic analysis. The surface and secreted .delta. chains of the IgD variant have apparent MW of 64,000 and 61,000, respectively. The unglycosylated secreted .delta. polypeptide chain has a MW of only 44,000. The secreted IgD exists predominantly in the .delta.2.lambda.2 form, does not contain J protein, is relatively stable in serum, and does not fix complement.

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