关键词: 植物螯肽合成酶, SrPCS1, 原核表达, 纯化

Abstract: In order to obtain purified Sesbania rostrata phytochelatin synthase1, the prokaryotic expressing vector pAM56 containing SrPCS1 open reading frame was constructed based on the vector pMAL-c2x and transferred into E. coli BL21(DE3) and induce the fusion protein MBP-SrPCS1.The fusion protein was then identified by western blotting and purified through Maltose Binding column.The results suggested that the soluble protein MBP-SrPCS1 was induced to express through 0.2 mmol/L of IPTG after 16 h at 15℃ and the purified MBP-SrPCS1 was obtained by affinity chromatography, which can lay a foundation for further study on the enzyme activity of SrPCS1 and the catalytic mechanism of PCS.

Key words: phytochelatin synthase, SrPCS1, prokaryotic expression, purification