Sequence of C region of L chains from Xenopus laevis Ig.
A cDNA expression library, prepared from Xenopus laevis splenocytes, was screened with antibodies to Xenopus Ig. One clone, lambda XIg23, reacted with antibodies to IgY and to IgM; the insert hybridized to approximately 1.3-kb RNA from spleen, the approximate size expected for L chain mRNA. An additional clone, lambda XIg31, was identified by cross-hybridization. The inserts of lambda XIg23 and lambda XIg31 begin in the third framework region of the V region and extend through the C region to the poly(A) tail. Except for a single nucleotide difference, the two C region sequences are identical. The amino acid sequence of the C region was compared with the sequences of a variety of C kappa and C lambda, as well as to C region sequences of L chains from Rana catesbeiana and from two species of shark. The Xenopus C region resembles mouse and human C kappa slightly more than C lambda. The similarity of the Xenopus and Rana C regions to each other is approximately the same as that of either amphibian sequence to mammalian CL. The data are discussed in terms of the evolution of kappa and lambda C regions.
Zezza
D J
DJ
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Mikoryak
C A
CA
Schwager
J
J
Steiner
L A
LA
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D004247:DNA / Q000302:isolation & purification; D007127:Immunoglobulin Constant Regions / Q000235:genetics*; D007147:Immunoglobulin Light Chains / Q000235:genetics*; D008969:Molecular Sequence Data; D011892:Rana catesbeiana; D014982:Xenopus laevis / Q000276:immunology*
D007127:Immunoglobulin Constant Regions; D007147:Immunoglobulin Light Chains; D004247:DNA