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Isolation and characterization of the nonpolysomal cytoplasmic messenger ribonucleoprotein complexes of rat liver.

Nonpolysomal cytoplasmic mRNA protein complexes (free mRNP) from normal and regenerating rat liver were isolated by affinity chromatography on oligo (dT)-cellulose column. The mRNP complexes bound to the oligo(dT) cellulose were eluted in a three-step process by using low ionic strength buffer (25 mM Tris–HCl, pH 7.5) at (i) 2 °C, (ii) 37 °C, and (iii) containing 50% formamide. The protein content of these three mRNP fractions, calculated from their buoyant densities, was found to be 50, 63, and 78%, respectively.Sixteen polypeptides of Mr 31 000 to 90 000 were present in these mRNP fractions. These polypeptides were found to be of nonribosomal origin. The polypeptide complements of these mRNP fractions were qualitatively similar when both major and minor components were considered. Considerable differences in the major polypeptides of the different mRNP fractions were observed. The major polypeptides of the mRNP eluted at 2 °C (mRNP-1) were of Mr equal to 51 000, 65 000, 74 000, 78 000, 80 000, 84 000, 8...