Molecular weight distribution of ribosomal proteins from several vertebrate species

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Abstract
Two-dimensional polyacrylamide gel electrophoresis of proteins from the separated ribosomal subunits of rabbit reticulocytes, rabbit liver, mouse liver, rat liver, chicken liver and toad liver was performed using the pH 4.5/sodium dodecyl sulfate system previously described, with internal standards to measure the molecular weight distributions. With few exceptions, the patterns were remarkably similar, indicating a high degree of conservation during evolution of both net charge (largely determining mobility in the 1st dimension) and size (determining mobility in the 2nd dimension). The aggregate mass (sum of molecular weights) of both small and large subunit proteins, about 0.65 .times. 106 and 0.95 .times. 106 daltons, respectively, were invariant. These figures are significantly smaller than the hydrodynamically determined mass of protein in the subunits. The implications of this discrepancy, which is opposite that found in the prokaryotes, is discussed.