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草鱼卵中蛋白酶抑制剂的初步分离及性质研究
Purification and Characteristics of a Trypsin Inhibitor from Ctenopharyngodon idellus Eggs
【摘要】 [目的]草鱼卵匀浆液中纯化获得蛋白酶抑制剂。[方法]采用Sephadex凝胶层析技术和发色底物检测,经分离与纯化获得具有专一性抑制活性的蛋白酶抑制剂。在不同温度(30~100℃)和酸碱(pH 2~11)条件下研究该抑制剂稳定性。[结果]从草鱼卵中分离到表观分子量50 kD的蛋白酶抑制剂,其对胰蛋白酶的最低抑制浓度约为500μg/ml,抑制常数为14.6 nmol/L。该蛋白酶抑制剂还具有高度的热稳定和酸碱稳定性。[结论]该研究可为淡水鱼卵的高效利用提供理论依据。
【Abstract】 [Objective] To obtain a protease inhibitor from eggs of Ctenopharyngodon idellus.[Method] By gel filtration chromatography and chromogenic substrate detection,a protease inhibitor which has specific inhibitory activity was obtained,and then its stability was studied through the change of temperature(30-100 ℃) and acid-base(pH 2-11) conditions.[Result] The purified inhibitor showed an apparent molecular weight of 50 kDa,and it potently inhibited trypsin with minimum inhibitory concentration of 500 μg/ml and a Ki value of 14.6 nmol/L,and also with a high degree of thermal stability and acid-base stability.[Conclusion] This study provides a theoretical basis for the efficient use of freshwater fish eggs.
【Key words】 Proteinase inhibitor; Inhibitory activity; Thermal stability; Acid-base stability;
- 【文献出处】 安徽农业科学 ,Journal of Anhui Agricultural Sciences , 编辑部邮箱 ,2012年26期
- 【分类号】S917.4
- 【下载频次】51