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Complete solubilization of ribosomal proteins during the fractionation of mouse liver ribosomal proteins by two-dimensional polyacrylamide gel electrophoresis.

Abstract When analyzing ribosomal proteins by two-dimensional polyacrylamide gel electrophoresis, insoluble stained material is usually seen remaining in the cylinder gel after electrophoresis in the second-dimension is complete. In addition, diners or high molecular weight aggregates are commonly seen on the second dimension slab gel, and they are not identified as ribosomal proteins. These artifacts are attributed to insolubility of the ribosomal proteins that occurs both prior to and during electrophoresis of these proteins. The procedure described here eliminates the solubility artifacts that occur during the preparation of liver ribosomal proteins for electrophoresis. Modifications are also made in the electrophoretic procedure to prevent dimer formation during electrophoresis. A four-celled slab gel apparatus, capable of analyzing 100–120 μg Tibosomal protein samples in 5 hours is also described. The 1.5 mm thick slab gels can be dried in 1 hour for autoradiography or storage.