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J. Biochem, 1977, Vol. 81, No. 4 941-947
© 1977 Japanese Biochemical Society

research-article

Purification of Immunoglobulin Light Chain Messenger RNA by Immunoprecipitation from Mouse Myeloma Tumor, MOPC-31C1

Masao ONO, Toshihiko KONDO and Masaya KAWAKAMI

Molecular Biology Laboratory, School of Medicine, Kitasato University Sagamihara, Kanagawa 228

Polysomes producing IgGl(k) myeloma protein were specifically selected by an immunoprecipitation method, and immunoglobulin light chain mRNA was purified from the precipitated polysomes. The purified mRNA migrated predominantly as a single band and the molecular weight of this mRNA was calculated to be 410,000 by polyacrylamide gel electrophoresis in 98% formamide. A protein possessing a molecular weight of 25,000, which is the size of the light chain precursor, was synthesized as a major product of translation in a wheat germ cell-free system. DNA complementary to the mRNA (cDNA) was prepared with avian myelo blastosis virus RNA-dependent DNA polymerase. This cDNA had an average size of 8.3S as determined by sedimentation through an alkaline sucrose gradient. Using this cDNA, CIt1/2 values of template RNA and RNA from various preparations were calculated from the results of molecular hybridization. The relative content of the mRNA increased 4.4-fold during the immunoprecipitation of polysomes.

1This study was supported in part by grants from the Ministry of Education, Science and Culture of Japan.


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