Molecular and General Genetics MGG

, Volume 162, Issue 3, pp 259–268

Yeast ribosomal proteins

I. Characterization of cytoplasmic ribosomal proteins by two-dimensional gel electrophoresis
  • E. Otaka
  • K. Kobata

DOI: 10.1007/BF00268851

Cite this article as:
Otaka, E. & Kobata, K. Molec. Gen. Genet. (1978) 162: 259. doi:10.1007/BF00268851


The cytoplasmic 80s ribosomal proteins from the cells of yeast Saccharomyces cerevisiae were analyzed by SDS two-dimensional polyacrylamide gel electrophoresis. Seventyfour proteins were identified and consecutively numbered from 1 to 74. Upon oxidation of the 80s proteins with performic acid, ten proteins (no. 15, 20, 35, 40, 44, 46, 49, 51, 54 and 55) were dislocated on the gel without change of the total number of protein spots. Five proteins (no. 8, 14, 16, 36 and 74) were phosphorylated in vivo as seen in 32P-labelling experiments.

The large and small subunits separated in low magnesium medium were analyzed by the above gel electrophoresis. At least forty-five and twenty-eight proteins were assumed to be in the large and small subunits, respectively. All proteins found in the 80s ribosomes, except for no. 3, were detected in either subunit without appearance of new spots. The acidic protein no. 3 seems to be lost during subunit dissociation.

Copyright information

© Springer-Verlag 1978

Authors and Affiliations

  • E. Otaka
    • 1
  • K. Kobata
    • 1
  1. 1.Department of Biochemistry and Biophysics, Research Institute for Nuclear Medicine and BiologyHiroshima UniversityHiroshimaJapan

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