Molecular and Cellular Biochemistry

, Volume 15, Issue 1, pp 67–71 | Cite as

Preparation of poly (A)-binding proteins from endoplasmic reticulum-containing subfractions of RAT liver cells and their use in mRNA purification

  • Bengt Axelsson
  • Rolf Ohlsson
  • Adam Deutsch
  • Bengt Jergil
Letters to the editor


Approximately 2% of the proteins solubilised from rat liver microsomes or rapidly sedimenting endoplasmic reticulum (RS-ER) adsorbed to poly(A)-Sepharose. The adsorption appeared to be selective for a few proteins, and proteins of different apparent molecular weights adsorbed from RS-ER and the microsomes. The proteins from RS-ER with affinity for poly(A) were coupled to Sepharose and used for the purification of mRNA from rabbit mammary glands. A portion of the RNA which did not adsorb to poly(U)-Sepharose adsorbed to protein-Sepharose and was active in a cell-free protein synthesis system.


Molecular Weight Endoplasmic Reticulum Protein Synthesis Liver Cell Mammary Gland 
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Copyright information

© Dr. W. Junk b.v. Publishers 1977

Authors and Affiliations

  • Bengt Axelsson
    • 1
  • Rolf Ohlsson
    • 1
  • Adam Deutsch
    • 1
  • Bengt Jergil
    • 1
  1. 1.Biochemistry 1Chemical CenterLund 7Sweden

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