Preparation of poly (A)-binding proteins from endoplasmic reticulum-containing subfractions of rat liver cells and their use in mRNA purification.
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 wihich did not adsorb to poly(U)-Sepharose adsorbed to protein-Sepharose and was active in a cell-free protein synthesis system.
D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism; D002846:Chromatography, Affinity; D003600:Cytosol / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005260:Female; D008099:Liver / Q000378:metabolism*; D008321:Mammary Glands, Animal; D008565:Membrane Proteins / Q000302:isolation & purification / Q000378:metabolism; D008862:Microsomes, Liver / Q000378:metabolism; D008970:Molecular Weight; D011061:Poly A / Q000378:metabolism*; D012333:RNA, Messenger / Q000302:isolation & purification / Q000378:metabolism; D051381:Rats; D013347:Subcellular Fractions / Q000378:metabolism
D002352:Carrier Proteins; D008565:Membrane Proteins; D012333:RNA, Messenger; D011061:Poly A