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Rabbit kappa-immunoglobulin chains exhibit diversity in the number of amino acids between the invariant residues Cys 88 and Phe 98; this length diversity is formally similar to that found in the human and mouse heavy chain systems, in which it results from interposition of the D element between V and J. To explore the molecular basis for this length diversity in rabbit kappa-chains we have determined the nucleotide sequence of a rabbit germline V kappa immunoglobulin gene. The spacing between the 7-mer and 9-mer signal elements of this gene suggest that it could recombine with J kappa without a D element. We discuss alternative explanations for the length diversity of rabbit kappa-chains.
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