食品科学 ›› 2003, Vol. 24 ›› Issue (7): 31-33.

• 基础研究 • 上一篇    下一篇

大豆中β-伴球蛋白的分离与纯化

 贾振宝, 郭(令鸟), 刘宁, 霍贵成   

  1. 东北农业大学食品学院
  • 出版日期:2003-07-15 发布日期:2011-12-13

 JIA  Zhen-Bao, GUO  (Ling-Niao-), LIU  Ning, HUO  Gui-Cheng   

  • Online:2003-07-15 Published:2011-12-13

摘要: 从大豆中分离制备β-伴球蛋白,对通过电泳进行分析鉴定。采用分级盐析(70%~90%)和凝胶过滤(Sepharose 6B)分离纯化大豆中的β-伴球蛋白。免疫电泳的结果证实所提取的β-伴球蛋白纯度很高,大豆中的其它成分与β-伴球蛋白抗血清无交叉免疫反应。SDS-PAGE的结果表明本实验所提取的β-伴球蛋白是由不同形式单体组成的复合物,共有6种亚基。

关键词: &beta, -伴球蛋白, 凝胶过滤, 纯化

Abstract: conglycinin in soybean was purified, and then assayed by electrophoresis. β- conglycinin in soybean wasprepared by salt precipitate (70%~90%) and gel filtration on a Sepharise 6B column. The result of immunoelectrophoresis illustratedthat the purified β- conglycinin was not contaminated,while the antiserum of β- conglycinin showed no cross-reaction withthe other proteins in soybean. The prepared β- conglycinin was heterogeneous based on SDS-PAGE, and was composed of sixkinds of subunits.

Key words: conglycinin, gel filtration, purification