Richer L L
Biochim Biophys Acta. 1978 Jan 26;517(1):76-83. doi: 10.1016/0005-2787(78)90035-7.
Rabbit globin alpha and beta chains were labeled with [3H]leucine, and with [35S] -methionine from reticulocyte tRNAMet isoacceptors using a rabbit reticulocyte cell-free synthesis system. [35S]Methionine from the three tRNAMet species isolated by RPC-5 chromatography was incorporated into internal positions of both alpha and beta globin. The initiator tRNA, tRNAIMet, exhibited very low efficiency for incorporating methionine internally, while tRNAIIMet was four times more efficient than tRNAIIIMet. 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-tRNAfMet showed a 3-fold increase over the reticulocyte initiator tRNA in its capacity to incorporate methionine into the internal positions of rabbit globin.
使用兔网织红细胞无细胞合成系统，用[³H]亮氨酸以及来自网织红细胞甲硫氨酸同工受体的[³⁵S] -甲硫氨酸对兔珠蛋白α链和β链进行标记。通过RPC - 5色谱法分离得到的三种甲硫氨酸转运核糖核酸（tRNAMet）中的[³⁵S]甲硫氨酸被掺入α珠蛋白和β珠蛋白的内部位置。起始转运核糖核酸（tRNAIMet）在内部掺入甲硫氨酸的效率非常低，而tRNAIIMet的效率比tRNAIIIMet高四倍。对标记珠蛋白的胰蛋白酶肽段进行氨基酸分析表明，所有三种同工受体都将甲硫氨酸掺入了正常的甲硫氨酸肽段中。用大肠杆菌[³⁵S]Met - tRNAfMet进行的类似研究表明，其将甲硫氨酸掺入兔珠蛋白内部位置的能力比网织红细胞起始转运核糖核酸高3倍。
