Abstract
A method for purification of the mRNA coding for heavy-chain protein of a mouse G2a myeloma (5563) is reported. Complete myeloma protein (H2L2) specifically binds to the heavy-chain mRNA, and the resultant RNA-protein complex is precipitated with antiserum against 5563 myeloma protein. Cytoplasmic RNA isolated by this method showed two bands of 6.0 × 105 and 3.1 × 105 molecular weight when analyzed by acrylamide gel electrophoresis. The RNA in the bands contained 1.5% and 8% A-rich regions, respectively. The RNA in each of the bands contained sequences for heavy-chain protein when translated in Xenopus laevis oocytes.
Keywords: myeloma, Xenopus laevis oocyte injection, antiserum, acrylamide gel electrophoresis
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