The accessibility of proteins of the Escherichia coli 30S ribosomal subunit to antibody binding |
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Authors: | G. Stö ffler, R. Hasenbank, M. Lü tgehaus, R. Maschler, C. A. Morrison, H. Zeichhardt R. A. Garrett |
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Affiliation: | (1) Abt. Wittmann, Max-Planck-Institut für Molekulare Genetik, Berlin-Dahlem |
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Abstract: | Summary The accessibility of each of the proteins on the E. coli 30S ribosomal subunit was established by investigating whether or not immunoglobulins (IgG's) and their monovalent papain fragments (Fab's), specific for each of the 21 single ribosomal proteins, bind to the 30S subunit. The interpretation of the results of five different experimental approaches, namely Ouchterlony double diffusion and immunological sandwich methods, sucrose gradient and analytical ultracentrifugation, and functional inhibition tests, indicate that all 21 proteins of the 30S subunit have determinants available for antibody binding. There were quantitative differences between the degree of accessibility of the different ribosomal proteins. An attempt was made to correlate the results with the protein stoichiometric data of the small subunit proteins. |
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