Abstract
Rabbit globin α and β chains were labeled with [ 3H]leucine, and with [ 35S]methionine from reticulocyte tRNA Met isoacceptors using a rabbit reticulocyte cell-free synthesis system. [ 35S]Methionine from the three tRNA Met species isolated by RPC-5 chromatography was incorporated into internal positions of both α and β globin. The initiator tRNA, tRNA Met I, exhibited very low efficiency for incorporating methionine internally, while tRNA Met II was four times more efficient than tRNA Met III. Amino acid analysis of the tryptic peptides of the labeled globins revealed that all three isoacceptors incorporated methionine into the normal methionine peptides. Similar studies with Escherichia coli [ 35S]Met-tRNA Met f showed a 3-fold increase over the reticulocyte initiator tRNA in its capacity to incorporate methionine into the internal positions of rabbit globin.
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