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Abstract
Abstract Two supernatant fractions, T1 and T2, have been isolated and partially purified from rat liver and rabbit reticulocytes. In a cell-free system programmed with polyuridylic acid, both fractions are needed for phenylalanine polymerization. T1 factor and GTP are required for the enzymatic binding of phenylalanil-tRNA to template charged ribosomes. In the course of the binding reaction, GTP is hydrolyzed while no dipeptide formation can be detected. T2 factor coincides with a ribosome-linked GTPase, which is not stimulated by the addition of polyuridylic acid and phenylalanil-tRNA.
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