Abstract
Publisher Summary This chapter describes the fractionation of rabbit fiver methionine tRNA species. At least three methionine acceptor activities were obtained by DEAE-Sephadex chromatography of crude liver tRNA. Only one of these tRNA Met species could be charged with E. coli synthetase and formylated with E. coli transformylase. All three tRNA Met species were further purified by passage through reverse-phase chromatography (RPC 3) and were obtained free from cross-contamination by the other methionyl tRNA species. The tRNA Met species was obtained in approximately 80% purity as judged by its methionine acceptor activity. The chapter concludes with a discussion on some properties of the methionyl-tRNA species. Attempts to charge other methionine-tRNA species with the E. coli enzyme under various conditions of magnesium ion and salt concentrations were unsuccessful. This fact has been used to charge preferentially the tRNA Met species present in crude tRNA preparations.
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