Abstract
Abstract Chloramphenicol inhibits binding of aminoacyl-oligonucleotides to ribosomes from Escherichia coli. These aminoacyl-oligonucleotides, C-A-C-C-A(Phe), C-C-A(Phe), C-C-A(Lys), C-C-A(Ser), and C-C-A(Leu), represent the aminoacyl-terminal fragments of aminoacyl-tRNA. Thus, it is possible that chloramphenicol inhibits the binding of this portion of aminoacyl-tRNA during its inhibition of protein synthesis. Of the four chloramphenicol enantiomers, only the active antibacterial isomer was effective. In addition, binding of [14C]chloramphenicol to ribosomes, studied by equilibrium dialysis, revealed two sites for chloramphenicol binding to ribosomes: a high affinity (Kdiss = 2 x 10-6 m) and a low affinity (Kdiss = 2 x 10-4 m) site. Many antibiotics were found to inhibit [14C]chloramphenicol binding: carbomycin, vernamycin A, lincomycin, gougerotin, sparsomycin, and puromycin. Puromycin appears to compete with chloramphenicol for similar or identical binding sites.
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