内蒙古大学艺术学院学报
內矇古大學藝術學院學報
내몽고대학예술학원학보
JOURNAL OF ART COLLEGE OF INNER MONGOLIA UNIVERSITY
2012年
4期
118-121
,共4页
李建云%张忠兵%王宇%范蒙光%刘芳%王鹏%胡艳红%李云章
李建雲%張忠兵%王宇%範矇光%劉芳%王鵬%鬍豔紅%李雲章
리건운%장충병%왕우%범몽광%류방%왕붕%호염홍%리운장
布鲁氏菌%bp26基因%重组质粒%表达
佈魯氏菌%bp26基因%重組質粒%錶達
포로씨균%bp26기인%중조질립%표체
Brucella%bp26 gene%recombinant plasnfid%expression
目的：克隆布鲁氏菌外膜蛋白bp26基因并构建原核表达系统。方法：用聚合酶链式反应技术扩增得到布鲁氏菌bp26基因片段，与PEASY—E1载体链接，转入B121（DE3）感受态细胞中，经IPTG诱导后，经SDS—PAGE检测重组蛋白表达，用Westernblot鉴定目的蛋白的生物活性。结果：DNA测序结果显示，重组质粒bp26基因的插入位点正确，成功构建了重组质粒PEASY—E1-bp26，经IPTG诱导，表达出大小为27kDa的bp26融合蛋白。结论：获得布鲁氏菌外膜蛋白bp26基因片段，并在大肠杆菌中表达出具有生物活性的bp26融合蛋白。
目的：剋隆佈魯氏菌外膜蛋白bp26基因併構建原覈錶達繫統。方法：用聚閤酶鏈式反應技術擴增得到佈魯氏菌bp26基因片段，與PEASY—E1載體鏈接，轉入B121（DE3）感受態細胞中，經IPTG誘導後，經SDS—PAGE檢測重組蛋白錶達，用Westernblot鑒定目的蛋白的生物活性。結果：DNA測序結果顯示，重組質粒bp26基因的插入位點正確，成功構建瞭重組質粒PEASY—E1-bp26，經IPTG誘導，錶達齣大小為27kDa的bp26融閤蛋白。結論：穫得佈魯氏菌外膜蛋白bp26基因片段，併在大腸桿菌中錶達齣具有生物活性的bp26融閤蛋白。
목적：극륭포로씨균외막단백bp26기인병구건원핵표체계통。방법：용취합매련식반응기술확증득도포로씨균bp26기인편단，여PEASY—E1재체련접，전입B121（DE3）감수태세포중，경IPTG유도후，경SDS—PAGE검측중조단백표체，용Westernblot감정목적단백적생물활성。결과：DNA측서결과현시，중조질립bp26기인적삽입위점정학，성공구건료중조질립PEASY—E1-bp26，경IPTG유도，표체출대소위27kDa적bp26융합단백。결론：획득포로씨균외막단백bp26기인편단，병재대장간균중표체출구유생물활성적bp26융합단백。
Objective:To clone and construct the recombinant expression plasmid for bp26 gene of Brucella in E. coll. Methods:The bp26 gene of Brucella was amplified from genomic DNA and cloned into PEASY - E1 vecor. The recombinant plasmid was then transformed into E. coli BL21 ( DE3 ). The expression of bp26 gene was induced by ITPG and the recombinant protein was identified by SDS -PAGE analysis. Results :The results of DNAs equencing showed that the sequence and cloning site of the inserted bp26 gene were correct, the recombinant expression plasmid PEASY- E1 -bp26 was 27kDa. Conclusion:The bp26 gene of Brucella are cloned and the recombinant bp26 protein are successfully expressed in E. coll.
