Abstract
Preparative amounts of formyl-methionyl-tRNA fmet, methionyl-tRNA fmet, and tRNA fmet were separated from each other with baseline resolution in 30 min using mixed-mode HPLC on hexanoic anhydride-modified aminopropylsilyl-Hypersil 2. Pure tRNA fmet was aminoacylated with [ 35S]methionine in the presence or absence of a formyl donor and was immediately fractionated on the column. Two isoacceptors, tRNA 1 fmet and tRNA 2 fmet, as well as aminoacyl-tRNA synthetases were clearly separated from each other. The purified f[ 35S]-methionyl-tRNA was biologically active in that as much as 98% could be bound to ribosomes in response to AUGUAA in vitro. Formyl-methionine was released from this complex by the action of termination factor and 92% of bound formyl-methionine was released by puromycin.
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