摘要
以重组的谷胱甘肽 S转移酶 ( G S T) 和目标蛋白的融合蛋白为靶, 通过将其固定于谷胱甘肽琼脂糖凝胶上, 可以方便地从噬菌体肽库中筛选目标蛋白的结合肽. 用此方法筛选到含 W W X F 结构的 H I V1 病毒蛋白 R( Vpr) 的结合肽, 与经典的将 Vpr 包被于培养板上的筛选方法相比, 此方法具有简便。
Recombinant glutathione S transferase (GST) Vpr fusion protein was used as target to select Vpr binding peptide from phage peptide library. By immobilized the GST or GST fusion protein to glutathione agarose gel, binding phage could be quickly panned and eluted by reduced glutathione. The sequencing result show that a WWXF motif exist among the Vpr binding peptide. Comparing with the classic biopanning method by coating target protein on plate this provide more quick and convenient way to screen binding protein from phage peptide library.
出处
《生物化学与生物物理进展》
SCIE
CAS
CSCD
北大核心
1999年第4期381-384,共4页
Progress In Biochemistry and Biophysics