Journal of Changshu Institute of Technology2012，Vol.26Issue(2)：66-70,5.
乌鳢鱼卵中胰蛋白酶抑制剂的分离纯化及性质研究
The Purification and Characterization of a Trypsin Inhibitor from Snakeheaded Fish（Ophicephalus argus）Eggs
摘要
Abstract
A protein with an apparent molecular weight of 42 kDa was purified from the egg of Snakehead （Ophi-cephalas argus） by gel filtration chromatography. The purified protein showed that a trypsin inhibitor activity with minimal critical concentration of inhibition was 130 μg/mL and potently inhibited trypsin with a Ki value of 30.3 nM. The research on its physics and chemistry nature indicates that the proteinase inhibitor has a very strong sup- pressing activeness to serine proteinase as well as a long-time thermal stability and an acid and alkali stability.关键词
蛋白酶抑制剂/丝氨酸蛋白酶抑制活性/耐热性/酸碱稳定性Key words
Ophicephalus argus/proteinase inhibitor/thermal stability/acid and alkali stability分类
农业科技引用本文复制引用
欧雪,袁卉华,刘铮兆,吴守亮,顾婷婷,韩曜平..乌鳢鱼卵中胰蛋白酶抑制剂的分离纯化及性质研究[J].Journal of Changshu Institute of Technology,2012,26(2):66-70,5.基金项目
江苏省大学生实践创新训练计划项目“几种鱼卵中蛋白酶抑制剂的理化性质研究” （）
