Abstract
A cell-free protein-synthesizing system from Proteus vulgaris was developed and characterized. Initially, a very low activity was found to occur; it was shown to be due to a deficiency in the endogenous transfer ribonucleic acid (tRNA) content of the cell extracts. When tRNA was added to the polyuridylic acid (poly U) directed system, incorporation of 14C-phenylalanine into polypeptide readily occurred. This incorporation was dependent on ribosomes and supernatant fraction and the optimum concentrations of the various components of the system were found to be as follows: 120 μg/ml tRNA, 30 mM magnesium, 0.5 mM spermidine, 60 mM potassium, 50 mM adenosine triphosphate (ATP), 5 mM guanosine triphosphate (GTP), 0.03 mM cytosine triphosphate (CTP) and uridine triphosphate (UTP), 5 mM phosphoenolpyruvate (PEP), 50 μg/ml poly U, and 30 mM 2-mercaptoethanol.
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