Abstract
Over 80% of the phenylalanyl-tRNA synthetase activity in Ehrlich ascites cell homogenates was found to be associated with the high speed particulate fraction. This enzyme activity occurred in two principle forms: activity bound to the ribosomes, and activity as part of a complex sedimenting at approximately 25S in a sucrose density gradient. The ribosome-associated enzyme was shown to be bound to the 60S ribosomal subunit. Exposure of the ribosomes to RNA resulted in removal of synthetase activity from the ribosomes and the concomitant appearance of activity in a complex sedimenting at 25S.
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