Protein S2 has been localized on the surface of the 30S subunit of Escherichia coli by immuno-electron microscopy. The antibody was obtained from a fusion of myeloma cells with spleen cells of mice, which had been immunized with intact 30S ribosomal subunits of E. coli. The binding site of the antibody was on the head of the small subunit, just above the small lobe, in the region where protein S3 has also been localized. S2 is the first ribosomal protein to have been mapped exclusively with monoclonal antibody

Schwedler-Breitenreuter, G., Lotti, M., Stöffler-Meilicke, M., Stöffler, G. (1985). Localization of ribosomal protein S2 on the surface of the 30S subunit from Escherichia coli, using monoclonal antibodies. EMBO JOURNAL, 4(8), 2109-2112 [10.1002/j.1460-2075.1985.tb03899.x].

Localization of ribosomal protein S2 on the surface of the 30S subunit from Escherichia coli, using monoclonal antibodies

Lotti, M;
1985

Abstract

Protein S2 has been localized on the surface of the 30S subunit of Escherichia coli by immuno-electron microscopy. The antibody was obtained from a fusion of myeloma cells with spleen cells of mice, which had been immunized with intact 30S ribosomal subunits of E. coli. The binding site of the antibody was on the head of the small subunit, just above the small lobe, in the region where protein S3 has also been localized. S2 is the first ribosomal protein to have been mapped exclusively with monoclonal antibody
Articolo in rivista - Articolo scientifico
Antibodies, Monoclonal; Antigen-Antibody Complex; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Immunoassay; Microscopy, Electron; Ribosomal Proteins; Ribosomes
English
1985
4
8
2109
2112
none
Schwedler-Breitenreuter, G., Lotti, M., Stöffler-Meilicke, M., Stöffler, G. (1985). Localization of ribosomal protein S2 on the surface of the 30S subunit from Escherichia coli, using monoclonal antibodies. EMBO JOURNAL, 4(8), 2109-2112 [10.1002/j.1460-2075.1985.tb03899.x].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/260241
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