摘要
克隆表达家蚕蚕蛹30 kD(1 kD=1 u)脂蛋白家族成员Bmlp7(Bombyx mori lipoprotein 7)的融合蛋白,鉴定其致敏原性.合成Bmlp7的基因后连接至载体质粒p MAL-C5e上,在大肠杆菌BL21中诱导表达出麦芽糖结合蛋白(maltose binding protein,MBP)-Bmlp7,纯化后,利用Western blot鉴定MBP-Bmlp7融合蛋白与家蚕过敏患者血清中特异性免疫球蛋白E(immunoglobulins E,Ig E)的结合能力.结果显示,纯化得到了纯度较高的MBP-Bmlp7融合蛋白,且该融合蛋白能够与家蚕过敏患者血清特异性IgE结合,说明Bmlp7是家蚕中一种潜在的致敏原.
The open reading frame of Bmlp7 from silkworm （Bombyx mori） was chemically synthesized and cloned into plasmid pMAL-c5e. The recombinant plasmid pMAL-Bmlp7 was transformed into E. coli BI21 and expressed as a fusion protein. The protein was purified using amylose affinity chromatography and purified to homogeneity. The immunoglobulins E （IgE） reactivity of the fusion protein was assayed by western blotting using sera of patient with silkworm allergies. The results show that the Bmlp7 fusion protein has IgE reactivity with the oatient sera.
出处
《深圳大学学报（理工版）》
EI
CAS
CSCD
北大核心
2017年第2期117-121,共5页
Journal of Shenzhen University(Science and Engineering)
基金
国家自然科学基金资助项目(81273275)
广东省科技计划资助项目(2014A020212422)~~
关键词
免疫学
家蚕
30
k
D脂蛋白
表达纯化
免疫印迹
融合蛋白
免疫原性
immunology
Bombyx mori
30 kD lipoprotein
expression and purification
immunoblotting
fusionprotein
immnogenicity
