Purification and translation of an immunoglobulin λ chain messenger RNA from mouse myeloma
- 29 June 1976
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 15 (13) , 2775-2779
- https://doi.org/10.1021/bi00658a011
Abstract
The 500-fold purification of an mRNA encoding an immunoglobulin .lambda. L chain derived from the mouse myeloma tumor, RPC-20 is described. Purification involves the isolation of membrane-bound polysomes, oligo(dT)-cellulose chromatography and sucrose gradient centrifugation under conditions favoring denaturation of polynucleotide complexes. The mRNA purified in this way directs the cell-free synthesis of a polypeptide which is 5 or 6 amino acids longer than the mature form of RPC-20 L chain. In addition to directing the synthesis of a precursor-like polypeptide, the mRNA migrates on electrophoresis as a band containing approximately 1150 nucleotides, about 500 more than required to encode the mature form of the L chain.This publication has 2 references indexed in Scilit:
- Quantitation of constant and variable region genes for mouse immunoglobulin λ. chainsBiochemistry, 1976
- A nuclease specific for heat-denatured DNA isolated from a product of Aspergillus oryzaeBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1966