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We have determined the amino acid sequence of the variable (V) region of the delta heavy (H) chain of human IgD isolated from the plasma of myeloma patient WAH. This V region is unusual in its amino end group (arginine) and in its length (129 residues). The length is due to 10 insertions in the third complementarity-determining region (CDR3). A computer search showed that no reported CDR3-joining region (-JH) sequences are identical and that they appear to be unrelated to the constant (C) region sequences of immunoglobulins. The V region sequence together with our previous results for the C region give the complete sequence of the human delta chain WAH, which has 512 amino acid residues and a Mr congruent to 65,000. The human delta chain has four domains (V, C delta 1, C delta 2, and C delta 3) and a long hinge region; by comparison, the mouse delta chain lacks a continuous segment of 135 residues, including half the hinge region and the entire C delta 2 domain. The human and mouse delta chains also differ in the number, kind, and location of GlcN and GalN glycans and probably in conformation and quaternary structure. These and other considerations suggest that there may be multiple forms of both secreted and membrane-bound IgD that differ in size, structure, and function.
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