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Analysis of mitochondrial ribosomal proteins of Saccharomyces cerevisiae by two dimensional polyacrylamide gel electrophoresis

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Summary

Proteins from mitochondrial ribosomes of Saccharomyces cerevisiae were analysed by a two dimensional gel electrophoresis method. Each ribosomal subunit revealed a reproducible characteristic pattern of protein components. The 37S small subunit contained 33 protein species with an average molecular weight of 27,300 daltons (ranging from 60,000 to 9500 daltons). The 50S large subunit showed 38 protein species with an average molecular weight of 23,000 (ranging from 41,000 to 10,000 daltons). Ribosomes from various sources were compared on the basis of protein composition.

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Authors and Affiliations

  1. Section de Biologie, Fondation Curie Institut du Radium, Bâtiment 110, F-91405, Orsay, (France)

    Gérard Faye & Frédéric Sor

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  1. Gérard Faye
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  2. Frédéric Sor
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Communicated by F. Kaudewitz

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Faye, G., Sor, F. Analysis of mitochondrial ribosomal proteins of Saccharomyces cerevisiae by two dimensional polyacrylamide gel electrophoresis. Molec. Gen. Genet. 155, 27–34 (1977). https://doi.org/10.1007/BF00268557

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  • DOI: https://doi.org/10.1007/BF00268557

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