摘要
等电点沉淀法和凝胶过滤层析提纯的β-伴大豆球蛋白经6mol·L-1脲变性后解聚为游离亚基,利用DEAE琼脂糖凝胶FF离子交换层析分离纯化β-伴大豆球蛋白亚基,并对纯化亚基进行透析复性。同时将β-伴大豆球蛋白免疫家兔制备抗血清,利用免疫印迹方法检测纯化的亚基与β-伴大豆球蛋白抗血清是否发生免疫反应。结果表明:利用DEAE琼脂糖凝胶FF阴离子交换层析可以纯化出高纯度的β-伴大豆球蛋白β亚基,纯化的β亚基可以与抗β-伴大豆球蛋白抗体结合,具有免疫活性。
Purified β-conglycinin prepared by electric-point precipitation and filtration chromatography was denatured by 6 mol · L^- 1 urea and separated into free subunits. The subunits of β- conglycinin were isolated and purified by DEAE- Sepharose F F anion exchange chromatography and the prepared subunits were renatured by dialysis. The rabbits were immunized by β-conglycinin to produce β-conglycinin special antiserum. The immune responses between purified subunits and the antiserum were determined by immunoblotting. The results indicated ： pure β subunit could be prepared from β- conglycinin by DEAE-Sepharose F F anion exchange chromatography, and the purified β subunit could specially bind to β-conglycinin antiserum and this oroved that the subunit had immunological activity.
出处
《大豆科学》
CAS
CSCD
北大核心
2009年第2期301-304,309,共5页
Soybean Science
基金
国家自然科学基金重点资助项目(30430520)
关键词
Β-伴大豆球蛋白
Β亚基
纯化
免疫活性
β- conglycinin
β subunit
Purification
Immunological activity
