Abstract
Fluorodinitrobenzene (FDNB), Woodward's reagent K, and cyanate were reacted in separate experiments with a crude mixture of Escherichia coli aminoacyl-RNA ligases. Each of these reagents was found to induce selective inhibition of the capacity of certain of these enzymes to esterify 14C-labeled amino acids to transfer RNA's. In particular, on treatment with FDNB, the arginyl-tRNA ligase activity was inhibited 88%, using conditions under which the lysyl-tRNA ligase activity was inhibited 20%. These ligases were amenable to purification, and this same preferential inhibition of the arginyl-tRNA ligase as compared to the lysyl-tRNA ligase was found to occur on treatment of these purified ligases with FDNB. The differential inhibitory effects on individual aminoacyl-RNA ligases varied from one reagent to another.
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