Abstract

ALTHOUGH chloramphenicol is known to inhibit microbial protein synthesis both in intact cells and in cell-free systems, protein synthesis in analogous mammalian systems has been, in general, resistant to inhibition by chloramphenicol. Recently, however, it was demonstrated that chloramphenicol can inhibit protein synthesis in mammalian cell-free systems as effectively as in analogous microbial systems when mammalian protein synthesis is stimulated by the addition of template RNA.1 It was suggested that chloramphenicol acts by blocking the attachment of messenger RNA to its ribosomal binding site. A similar explanation was offered by Ambrose and Coons,2 who demonstrated the ability of chloramphenicol to . . .

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