A specially designed apparatus and conditions are described for the rapid analysis of ribosomal proteins by two-dimensional gel electrophoresis on a micro scale. The resolution of proteins in electropherograms is comparable to that obtained with other systems, but because of miniaturization, only 0.
Analysis of mitochondrial ribosomal proteins of Saccharomyces cerevisiae by two dimensional polyacrylamide gel electrophoresis
✍ Scribed by Faye, G�rard ;Sor, Fr�d�ric
- Publisher
- Springer
- Year
- 1977
- Tongue
- English
- Weight
- 664 KB
- Volume
- 155
- Category
- Article
- ISSN
- 0026-8925
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✦ Synopsis
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 95000 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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The 80S ribosome of Schizosaccharomyces pombe contains 93 proteins as determined by twodimensional electrophoresis on polyacrylamide gels. Of these, 76 are basic and 17 are acidic at pH 8.7. 38 proteins could be assigned unambiguously to the large sub-unit and 19 to the small. 67 proteins were extra