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The ribosomal proteins fromE. coli strains B, C, K12 (A19), and MRE600 were extracted and analyzed by two-dimensional polyacrylamide gel electrophoresis. All four strains were found to be indistinguishable in their 50S ribosomal protein components, while there were differences among the 30S proteins. Strains K and B differ in protein S5 and S7. Strain C differs from strain B in protein S5 and from strain K in protein S7. MRE600 appears to be identical to strain C in respect to its ribosomal protein pattern. It was furthermore found that proteins S7 from strain K and B differ extensively in respect to size, charge, amino acid composition and immunological properties. The rather remote relationship between these two analogous proteins is quite remarkable when contrasted with the striking similarity in all but one of the other 30S and 50S proteins of the strains.
KeywordsElectrophoresis Acid Composition Polyacrylamide Ribosomal Protein Amino Acid Composition
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- Kaltschmidt, E.: Ribosomal proteins, XIV. Determination of isoelectric points of ribosomal proteins ofE. coli by two-dimensional gel electrophoresis. Manuscript submitted for publication in Analyt. Biochemistry (1971).Google Scholar