核黄素受体蛋白的原核融合表达  

Prokaryotic Expression of a Riboflavin Binding Protein

作　　者：贾琴[1] 顾甘雨[1] 吴晓静[1] 林玲[1] 宋韬[1] 董汉松[1] 

机构地区：[1]南京农业大学植物保护学院,江苏南京210095

出　　处：《鲁东大学学报（自然科学版）》2007年第2期164-167,共4页Journal of Ludong University:Natural Science Edition

基　　金：教育部科学技术研究重点项目(03170)

摘　　要：用PCR(polymerase-chain-reaction)方法从含有软体海龟编码核黄素结合蛋白(riboflavin binding protein,RfBP)基因的质粒中克隆出RfBP基因,将该基因与原核表达载体pET30a(+)重组并研究了表达条件,聚丙烯酰胺凝胶(SDS)电泳表明,蛋白质的大小为35 kD,以BL21(DE3)pLysS作宿主菌,1 mmol/LIPTG(isopropyl-l-thio-β-D-galactoside)诱导4h,融合蛋白His-tag-RfBP表达量达到最大.本文研究结果可为研究核黄素受体蛋白调节植物的核黄素含量及生长发育机制奠定基础.Polymerase-Chain-Reaction(PCR) protocol was used to amplify the riboflavin binding protein gene(RfBP).It s cDNA was cloned in the prokaryotic expression vector pET30a(+) and the expressing conditionswere studied.Sodium dodecyl sulphate polyacrylamide gel electrophoresis(SDS-PAGE) showed that the size of the exogenous protein was approximately 35 kD;using the Escherichia coli BL21(DE3)pLysS,with 1 mmol/l IPTG inducing 4 hours,the his-tagged RfBP fusion protein wss expressed well at 37 C.These results may pro...

关 键 词：核黄素受体蛋白 原核表达 聚丙烯酰胺凝胶电泳 

分 类 号：Q78[生物学—分子生物学]