Preparation and characterization of two monoclonal antibodies against different epitopes in Escherichia coli ribosomal protein L7/L12

Autor:	G. R. Gavino, Robert R. Traut, A Sommer, C Casiano, N Zecherle, J R Etchison
Rok vydání:	1985
Předmět:	biology medicine.drug_class Protein subunit Cell Biology Ribosomal RNA Monoclonal antibody Biochemistry Primary and secondary antibodies Ribosome Molecular biology Epitope Elongation factor Affinity chromatography biology.protein medicine Molecular Biology
Zdroj:	Journal of Biological Chemistry. 260:6522-6527
ISSN:	0021-9258
DOI:	10.1016/s0021-9258(18)88812-3
Popis:	Two monoclonal antibodies with specificities for Escherichia coli 50 S ribosomal subunit protein L7/L12 were isolated. The antibodies and Fab fragments thereof were purified by affinity chromatography using solid-phase coupled L7/L12 protein as the immunoadsorbent. The two antibodies were shown to recognize different epitopes; one in the N-terminal and the other in the C-terminal domain of protein L7/L12. Both intact antibodies strongly inhibited polyuridylic acid-directed polyphenylalanine synthesis, ribosome-dependent GTPase activity, and the binding of elongation factor EF-G to the ribosome. Ratios of antibody to ribosome of 4:1 or less were effective in inhibiting these activities. Neither antibody prevented the association of ribosomal subunits to form 70 S ribosomes. The Fab fragments showed similar effects.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::b3c2628be2346f90dd7dcf20c7e2d6c1 https://doi.org/10.1016/s0021-9258(18)88812-3 Zobrazit plný text záznamu