Protein-deficient ribosomal particles from yeast 60S subunits obtained by modification with dimethylmaleic anhydride and by treatment with NH4Cl

Abstract

The protein-deficient particles prepared from yeast 60S subunits by modification of lysine residues with the reversible reagent dimethylmaleic anhydride are compared with those obtained by treatment with NH4Cl.The two procedures cause selective dissociation of certain proteins.With a few exceptions, the dissociation pattern is similar in both cases.When using dimethylmaleic anhydride, a variation in the protein composition of the ribosomal cores is obtained by modification of the ribosomal subunits in the presence of any of the following ligands: elongation factor-2, ricin A, verrucarine A and puromycine.