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引用次数: 4
摘要
利用L/ f - trna -蛋白转移酶在温和的酶促反应条件下，实现了以赖氨酸为n端残基的蛋白质(Lys-XBD)的n端特异性放射性同位素(RI)标记。为了仅在n端暴露单个赖氨酸片段，我们使用细菌表达宿主BL21(DE3)过表达pelB信号肽-赖氨酸- xbd融合蛋白。pelB信号肽在大肠杆菌中自发裂解得到所需的Lys-XBD。
Leucyl/phenylalanyl (L/F)-tRNA-protein transferase-mediated N-terminal specific labelling of a protein in vitro.
N-terminal specific radioisotope (RI) labelling of a protein posessing lysine as the N-terminal residue (Lys-XBD) was achieved under mild enzymatic reaction condition using L/F-tRNA-protein transferase. To expose a single lysine moiety only at the N-teminal site, we overexpressed pelB signal peptide-Lys-XBD fusion protein using the bacterial expression host BL21(DE3). The pelB signal peptide was sponteneously cleaved in E. coli to obtain the desired Lys-XBD.
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