Abstract
Ribosomal proteins from pure free and membrane-bound rat liver polysomes were analyzed with a highly resolutive two-dimensional gel electrophoresis technique, using sodium dodecyl sulfate in the second dimension. Three acidic proteins found in free polysomes were always absent from the membrane-bound polysomes. Their molecular weights were estimated to be 20 000, 19 500 and 18 500. When free ribosomes were dissociated into subunits, the three protein spots were still found in the 60S subunit pattern, but they were weaker than in polysomes. A possible involvement of these three proteins in the attachment of ribosomal structures to the membranes is proposed.
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