Hybrid selection of messenger ribonucleoprotein for serum albumin: analysis of specific message-bound proteins

Abstract

The messenger RNA for chicken serum albumin together with its specific binding proteins was purified by hybrid selection using filter-bound cloned albumin cDNA. Under conditions where hybridization of the protein-mRNA complex was specific for the immobilized cDNA sequence, no dissociation of the complex into its protein and RNA components was apparent. Electrophoretic analysis of albumin mRNA-specific binding proteins showed three major bands. Two of these were prominent in total poly(A) messenger ribonucleoprotein. The third band was of much greater relative intensity in the albumin mRNA-specific proteins than in total poly(A) messenger ribonucleoprotein. The results suggest that the proteins bound to albumin mRNA represent only a subset of the total population of poly(A) mRNA-associated protein.