BASILEA rabbits express two types of immunoglobulin light chains: lambda and kappa-like.

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Abstract
In the variant rabbit strain BASILEA, IgG were shown to contain 2 distinct populations of IgG molecules whose L chains belonged to the known .lambda. isotype and to a new .kappa.-like type. These 2 L chains differed from each other by electrophoretic, chemical, and antigenic properties. The .kappa.-like L chain fraction showed an acid-labile Asp-Pro bond at the end of the joining region and a tryptic peptide, whose amino acid sequence of the NH2-terminal 15 residues was identical to the homologous constant (C) region sequence of b9 .kappa. chain with the exception of the residue in position 70, which is asparagine in the .kappa.-like chain instead of the characteristic half-cystine residue in all L chains of .kappa.B type expressing b4, b5, b6 or b9 allotypes. The .kappa.-like L chain component apparently does not contain the C region half-cystine residue involved in the formation of the extra variable (V) region-C region disulfide bridge in L chains of the .kappa.B type. The partial NH2-terminal amino acid sequence of the C region of the .kappa.-like L chain was shown to be markedly different from b4, b6 or b9 region sequences and from rabbit .lambda. C region sequence. The .kappa. bas component appears to represent a new subtype of .kappa. chain. A rabbit alloantiserum made against bas IgG and adsorbed with IgG fractions showing b4, b5, b6, b95 and b96 L chain allotypes appeared to be directed against the .kappa.-like L chain component of BASILEA IgG exclusively. All BASILEA animals expressed IgG molecules containing .kappa.-like chains; IgG molecules derived from the standard domestic rabbit did not react with this antiserum.