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长喙田菁植物螯合肽合成酶PCS2的原核表达及纯化
引用本文:李安明,邓青云,李德华. 长喙田菁植物螯合肽合成酶PCS2的原核表达及纯化[J]. 甘肃农业大学学报, 2011, 46(6): 150-154
作者姓名:李安明  邓青云  李德华
作者单位:孝感学院生命科学技术学院,湖北孝感,432000
基金项目:湖北省重点(培育)学科:农业资源利用,湖北省自然科学基金项目
摘    要:为了获得纯化的长喙田菁(Sesbania rostrata)植物螯合肽合成酶PCS2,以原核表达载体pMAL-c2x为基础,构建了含有SrPCS2开放阅读框序列的原核表达载体pAM57,将其转化表达菌株BL21 (DE3),对融合蛋白的表达进行了优化,通过Western blotting鉴定融合蛋白,并用麦芽糖亲和柱对...

关 键 词:植物螯肽合成酶  SrPCS2  原核表达  纯化

Expression and purification of Sesbania rostrata phytochelatin synthase2 in Escherichia coli
LI An-ming,DENG Qing-yun,LI De-hua. Expression and purification of Sesbania rostrata phytochelatin synthase2 in Escherichia coli[J]. Journal of Gansu Agricultural University, 2011, 46(6): 150-154
Authors:LI An-ming  DENG Qing-yun  LI De-hua
Abstract:The mature peptide of Sesbania rostrata phytochelatin synthase2(SrPCS2) was subcloned into pMAL-c2x vector to construct the prokaryotic expression vector pAM57.The recombinant plasmid was transformed into E.coli BL21(DE3),then the fused protein MBP-SrPCS2 was induced by IPTG at different temperature,identified by Western blotting and purified through Maltose Binding column.The results suggested that the soluble fusion protein MBP-SrPCS2 was expressed at high levels 16 h after 0.2 mmol/L of IPTG induction(15℃) and the purified MBP-SrPCS2 was obtained by affinity chromatography.
Keywords:phytochelatin synthase  SrPCS2  prokaryotic expression  purification
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