A Comparison of the Proteins of Rat Skeletal Muscle and Liver Ribosomes by Two-Dimensional Polyacrylamide Gel Electrophoresis OBSERVATIONS ON THE PARTITION OF PROTEINS BETWEEN RIBOSOMAL SUBUNITS AND A DESCRIPTION OF TWO ACIDIC PROTEINS IN THE LARGE SUBUNIT

摘要: Abstract We have determined the number of proteins in rat skeletal muscle 80 S ribosomes and ribosomal subparticles by two-dimensional polyacrylamide gel electrophoresis. The were compared with those from liver ribosomes. small subunit contained 31 proteins: it had two (Sm1 Sm2) which not found 40 particles; one protein (S31*) was always but present subparticle only if they prepared buffer containing 500 mm potassium 3 magnesium (it absent cation concentrations during preparation 830 12.5 mm, respectively); lacked S10 S22; finally, S8 subunits lower (500 mm) whereas concentration higher (830 magnesium). large 38 (L1 L41*) that 60 subunits; (L20) magnesium; L20 is also are potassium. detected acidic (L40* may be homologous Escherichia coli L7 L12. Preparations monomers five (1, 2, 3, L1, M4) either subunit; (M4) estimate 67 to 74 different proteins; 69 74. Most apparent variance between can accounted for differential partition selected or other subunits, differences methods required prepare pure high yield used Thus certain occur vice versa. If same method there few any proteins.