Abstract
A factor which promotes the binding of Phe-tRNA to 40-S ribosomal subunits has been isolated from rat liver cytosol and considerably purified by DEAE-cellulose and hydroxylapatite chromatography. The molecular weight of the factor was estimated to be about 93 000 by chromatography on Sephadex G-200. Binding of Phe-tRNA to 40-S ribosomal subunits, catalyzed by the purified factor, required polyuridylic acid but not GTP; the latter in contrast to previous results with a crude preparation. Factor dependent binding to puromycin-stripped ribosomes (‘80 S’) was less than half that to an equimolar quantity of 40-S subunits and the addition of 60-S subunits caused a partial inhibition of the binding to 40-S subunits. The factor also directed the binding of fMet-tRNA and N-acetyl-Phe-tRNA to 40-S subunits. It is suggested that the factor may be the same as the recently described reticulocyte initiation factor M1.
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