巴豆毒蛋白的分离、结晶及其性质研究  

Isolation,Characterization and Crystallization of Crotins Toxin from the Seeds of Croton tiglium L.

作　　者：陈明晃[1] 潘克桢[1] 

机构地区：[1]中国科学院福建物质结构研究所,福州350002

出　　处：《生物化学杂志》1993年第1期104-108,共5页

基　　金：国家自然科学基金;福建省自然科学基金

摘　　要：巴豆种子用PBS抽提,多次低溫离心去除大量油脂,经硫酸铵沉淀,从Sophadex G-75柱分离出巴豆毒蛋白Ⅰ和Ⅱ(CrotinⅠ,Ⅱ)SDS-PAGB测得其分子量为40kD和15kD;等电点分别为8.0和6.7,并测定了它们的氨基酸组成。巴豆毒蛋白Ⅱ用汽相扩散悬滴法获得结晶,蛙卵试验表明它具有较强的抑制蛋白质合成的活性。Two toxins, Crotin Ⅰ, Ⅱ were isolated from the seeds of Croton tiglium by extraction with PBS, precipitation with ammonium sulfate followed by gel filtration through Sephadex G-75. The molecular weights estimated by SDS-PAGE were 40kD and 15kD and the isoelectric point estimated to be 8.0 and 6.7, respectively. The acute LD_(50) evaluated at 72h was 0.45 mg/mouse for Crotin Ⅰ and 2.23mg/mouse for Crotin Ⅱ. Crotin Ⅱ strongly inhibits protein synthesis in eukaryotic ribosome by oocyte of the toad test and belongs to Ribosome-inactivating Proteins. Crotin Ⅱ was crystallized by hanging droplet method.

关 键 词：巴豆 毒蛋白 分离 结晶 

分 类 号：Q946.1[生物学—植物学]