Abstract
Oligolysyl-tRNA, synthesized in cell-free extracts from Escherichia coli, was deacylated by four methods: alkaline hydrolysis (pH 9.6), proteolytic digestion with trypsin, peptide donation to puromycin and hydrolysis stimulated by partially purified peptidyl-tRNA hydrolase. Regardless of the method of deacylation the tRNA product could accept the expected amount of lysine. After the mild alkaline hydrolysis the tRNA product was shown to be able to participate in further rounds of peptide synthesis.
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