Abstract

The separation of rat liver and E. coli ribosomal subunits was attempted on Trisacryl GF 2000. Contrary to experiments with Sepharose 4B and Bio-Gel A-15 the 60S mammalian subunit did not bind to the resin at 4°C but eluted within the column volume ahead of the 40S subunit. Puromycin however used to prepare the subunits which on the agarose gels had eluted at the total column volume exhibited anomalous retardation on the Trisacryl resin. Trisacryl therefore behaves as the more non-polar resin and the binding of 60S subunits to agarose gels is a result of hydrophilic interaction.

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