Effect of Chloramphenicol on Enzyme Synthesis and Growth of Mammalian Cells

D-threo-Chloramphenicol and its sulfamoyl analogue Tevenel, but not L-chloramphenicol, prevent the formation of a functional cytochrome c oxidase in L cells. The syntheses of several mitochondrial enzymes, malate dehydrogenase, succinate dehydrogenase, NADH dehydrogenase, ATPase, and cytochromes b, c, and c1, were not inhibited. Cycloheximide also inhibited the formation of cytochrome c oxidase. After removal of D-chloramphenicol or Tevenel, cytochrome oxidase activity returned at a rate equivalent to its normal synthesis. L cells continued to grow for up to five generations in the presence of Tevenel at 100 μg/ml but only for 1.5 to two generations with D-chloramphenicol at the same concentration. D-Chloramphenicol specifically inhibited the synthesis of insoluble mitochondrial proteins in ascites cells.