Abstract
The RNase inhibitor from 100,000 g rat liver supernatant fraction has been purified 3000–4000-fold by ammonium sulfate fractionation, DEAE-Sephadex A-50 chromatography, and gel filtration on Sephadex G-100. Purification of the inhibitor is paralleled by a concomitant purification of the factor which stabilizes the polysomal profile on sucrose gradients. This is also reflected by amino acid incorporation ability of the polyribosomes. Increasing purity of the factor is associated with increasing lability.
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