Amino acid sequence of the constant region of immunoglobulin light chains from Rana catesbeiana

Little is known about the detailed structure of immunoglobulins in non-mammalian vertebrates. We have determined the amino acid sequence of the constant region of immunoglobulin light chains from the bullfrog, Rana catesbeiana. There appears to be one major type of light chain in this species. However, at position 153, about half of the chains have lysine, the remainder having arginine. Variation at this same or at an adjacent position is responsible for allotypic or isotypic variation in human kappa and lambda chains. At three positions (118, 119, and 181), residues that occur in all known kappa and lambda chains in other species are replaced in the Rana catesbeiana sequence. One of these unusual substitutions--the replacement of proline by cysteine at position 119--allows the formation of an extra intrachain disulfide bond within the constant domain, between positions 119 and 214. This bond appears to replace the usual disulfide bridge between heavy and light chains so that, in the immunoglobulins of this species, the light chains are not covalently bonded to heavy chains. The sequence of the Rana catesbeiana constant region is compared to sequences of a variety of mammalian light chain constant regions. We consider the implications of these comparisons for the timing of the divergence of kappa and lambda chains relative to the divergence of the lineages leading to amphibians and to mammals and birds.