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蓖麻毒蛋白的分离纯化和毒理作用研究
作者姓名:曾佑炜  宋光泉 彭永宏  徐杰  梁关生
作者单位:广东轻式职业技术学院食品与生物工程系 广州510300 (曾佑炜,彭永宏),华南师范大学生命科学学院广东省植物发育生物工程重点实验室 广州510631 (宋光泉,徐杰),仲恺农业技术学院 广州510225(梁关生)
基金项目:广东省自然科学基金资助项目(011065)
摘    要:经(NH4)2SO4沉淀,分子筛层析和亲和层析等处理,从去壳蓖麻籽中分离纯化得到蓖麻毒蛋白,在SDS-聚丙烯酰胺凝胶电泳中呈32kDa和34kDa两条蛋白带,证明该蓖麻毒蛋白已被纯化至均一。用等电聚焦法测出该蓖麻毒蛋白的等电点为pI6.1和pI6.7。高效液相色谱测出该蓖麻毒蛋白在非变性条件下有五个峰,表明蓖麻毒蛋白可能存在五个不同的多聚态。动物实验表明该蓖麻毒蛋白对小白鼠有较强的毒性,但对斜纹夜蛾幼虫无毒杀作用。

关 键 词:蓖麻毒蛋白  亚基组成  等电点  高效液相色谱  毒杀作用

Purification and toxicity characterization of Ricin from Ricinus communis beans
Authors:Zeng Youwei  Peng Yonghong  Song Guangquan  Xu jie  liang guansheng
Institution:(1 College of Life Science, South China Normal University, Guangdong Key Lab of Biotechnology for Plant Development Guangzhou, 510631, China) (2. Application Chemistry Research Center, Zhong-kai Agricultural technical College, Guangzhou, 510225, China)
Abstract:Ricin was purified from Ricinus communis beans to apparent homogeneity by ammonium sulfate precipitation, Sepharose-4B affinity chromatography, and fllowed by molecular sieve chromatography. The purified preparation showed two protein bands with relative molecular weights of 32 kDa and 34kDa when subjected to sodium dodecyl sulfate-polyacrylamide gel eloctrophoresis.The isoelectric point of the purified Ricin was pI6.1 and pI6.7 determined by isoelectric focusing (IEF).There were five peaks when Ricin was subjected to high performance liquid chromatography (HPLC) under non-denaturing conditions, indicating this Ricin consisted of five different multimers. Purified Ricin revealed high toxicity to mouse, but had no any toxicity to Prodenia litura Fabricius larvae.
Keywords:Ricin  Subunit  pI  HPLC  Toxicity
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