Abstract
Extracts prepared from native ribosomal subunits of rat liver with high salt (0.5 m KCl) solutions contain dissociation factor activity; they dissociate 80 S ribosomes and prevent the reassociation of ribosomal subunits. One of the activities is a high molecular weight (500,000–700,000) protein composed of about 10 polypeptides (eIF-3 H). A low molecular weight activity (eIF-3 L) is resolved from the heavy dissociation factor by glycerol gradient centrifugation. Both activities catalyze dissociation and anti-association. Gel electrophoresis of complexes between ribosomal subunits and eIF-3 L, in sodium dodecyl sulfate, suggests that the low molecular weight dissociation factor contains a polypeptide or polypeptides of 51,000 molecular weight. Comparison of the electrophoretic patterns does not reveal any common polypeptides in the two dissociation factor preparations.
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