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Amino acid sequence of heavy chain from Xenopus laevis IgM deduced from cDNA sequence: implications for evolution of immunoglobulin domains.
Schwager J, Mikoryak CA, Steiner LA.
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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 lambda gt11 from mitogen-stimulated splenocytes of this species. Of approximately equal to 50,000 clones screened, 18 were found to express IgM epitopes. One of these, lambda XIg14, hybridized with RNA of RNA of approximately equal to 2 kilobases from splenocytes. The insert of this clone appears to encode a variable region and part of a mu constant region; that of another clone, lambda XIg8, appears to encode a variable region and a complete mu constant region. Both inserts contain sequence corresponding to the three gene segments (VH, DH, and JH) that encode heavy-chain variable regions. The heavy-chain constant region (CH) encoded by lambda XIg8 has the characteristic features of C mu, including a four-domain structure and a carboxyl-terminal tail. The amino acid sequences of two mu-chain peptides agree with the cDNA sequence. The identity in amino acid sequence between the corresponding Xenopus and mouse C mu domains ranges from 31 to 47%. The C mu 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.
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