Study of the interaction of Escherichia coli methionyl-tRNA synthetase with tRNAfMet using chemical and enzymatic probes.
Study of the interaction of Escherichia coli methionyl-tRNA synthetase with tRNAfMet using chemical and enzymatic probes.
复制标题
使用化学和酶探针研究大肠杆菌甲硫氨酰-tRNA 合成酶与 tRNAfMet 的相互作用。
DOI：
10.1021/bi00363a042
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发表时间：
1986
期刊：
影响因子：
2.9
通讯作者：
Schulman,LH
中科院分区：
文献类型：
--
作者：
Pelka,H;Schulman,LH
Methods 5'and 3'End Labeling of tRNAMa. tRNA™" was dephosphorylated by incubationwith calf intestinal phosphatase at 65 C and labeled with 32P at the 5'terminus by incubation with T4 polynucleotide kinase and [7-32P] ATP at 37 C, as described elsewhere (Schulman et al., 1983). The 3'-terminal adenosine residue of tRNA™" was labeled with 32P by using an exchange reaction catalyzed by E. coli tRNA nucleotidyl transferase in the presence of [a-32P] ATP and sodium pyrophosphate, as described by Francis et al.(1983).
