The identification of messenger RNA coding for immunoglobulin heavy and light chains of Xenopus laevis.
Total poly(A)-containing mRNA isolated from Xenopus spleens was translated in a rabbit reticulocyte lysate in vitro protein-synthesizing system. Approx. 1% of the radioactivity incorporated into the protein was precipitated by an antibody directed against adult Xenopus IgM. The immunoprecipitated proteins were characterized as IgM heavy and light chains by their molecular weight as determined by polyacrylamide-sodium dodecyl sulfate gel electrophoresis The sequence variability of the synthesized light c hain proteins was analyzed by isoelectric focusing and shown to be indistinguishable from authentic Xenopus immunoglobulin light chain proteins derived from IgM. The data presented here identify Xenopus spleen mRNA as a potential source of a natural immunoglobulin mRNA population with which the development of the immune system can be studied.
D000595:Amino Acid Sequence; D000818:Animals; D002474:Cell-Free System; D011232:Chemical Precipitation; D007143:Immunoglobulin Heavy Chains / Q000096:biosynthesis; D007147:Immunoglobulin Light Chains / Q000096:biosynthesis; D007075:Immunoglobulin M / Q000096:biosynthesis*; D007158:Immunologic Techniques; D007525:Isoelectric Focusing; D008970:Molecular Weight; D011061:Poly A / Q000378:metabolism; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism*; D011817:Rabbits; D013154:Spleen / Q000378:metabolism; D014981:Xenopus
D007143:Immunoglobulin Heavy Chains; D007147:Immunoglobulin Light Chains; D007075:Immunoglobulin M; D012333:RNA, Messenger; D011061:Poly A