Abstract
Ribosomal proteins from Xenopus laevis ovary have been analysed in one dimensional and two dimensional polyacrylamide gels, in comparison with proteins from Escherichia coli and rabbit reticulocyte ribosomes. The number average molecular weights of Xenopus and rabbit reticulocyte ribosomal proteins are similar (20·10 3), compared with 16·10 3 for the proteins of E. coli ribosomes. The total number of protein molecules from Xenopus ovary ribosomes exceeds that present in E. coli; a total of 30–40 protein molecules were obtained from the small subparticle and 60–70 from the larger subparticle of Xenopus. However, when subjected to two dimensional electrophoresis 26–28 different protein species were obtained from the smaller subparticle and no more than 37 different species from the larger subparticle of Xenopus. It appears therefore, that the majority of proteins from the smaller subparticle of Xenopus ribosomes are present as one copy per ribosome, whereas some proteins of the larger subparticle are present as more than one copy per ribosome.
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