Present understanding of the evolution of immunoglobulins is derived almost entirely from studies of a few mammalian species. To obtain information about immunoglobulin genes in Xenopus laevis, a cDNA library was prepared in the expression vector Agtll from mitogen-stimulated splenocytes of this species. Of =50,000 clones screened, 18 were found to express IgM epitopes. One of these, AXIg14, hybridized with RNA of :2 kilobases from splenocytes. The insert of this clone appears to encode a variable region and part of a ,I constant region; that of another clone, AXIg8, appears to encode a variable region and a complete ,u constant region. Both inserts contain sequence corresponding to the three gene segments (VH, DH. and J.) that encode heavy-chain variable regions. The heavy-chain constant region (CH) encoded by AXIg8 has the characteristic features of CIA, including a four-domain structure and a carboxyl-terminal tail. The amino acid sequences of two ,u-chain peptides agree with the cDNA sequence. The identity in amino acid sequence between the corresponding Xenopus and mouse C,, domains ranges from 31 to 47%. The C, domains vary in the extent to which their sequences resemble the sequences of other immunoglobulins, consistent with previous suggestions that the immunoglobulin domains have an independent evolutionary history.