摘要
通过硫酸铵分段沉淀、DEAE-32纤维素柱和SephadexG-75柱层析,从福寿螺(Ampullarum crossean)体内分离纯化出一种相对分子质量约为40kDa的纤溶活性蛋白,紫外光谱法测定表明,该蛋白具有纤溶作用,经SDS-PAGE电泳显示为一条带。研究表明,该蛋白作用最适pH为8.0,最适温度为59℃,热稳定性较好,金属离子Na+对酶的活力无影响,而K+、Mg2+、Ca2+可提高此蛋白酶的活力。采用平板法测定此蛋白酶的血纤维蛋白溶解活性,证明此酶具有强烈的纤溶活性。
A novel fibrinolytic protein has been separated and purified by ammonium sulfate fractionation,DEAE-32 cellulose and SephadexG-75 column chromatography from the Ampullarum crossean in the paper.The protein showed an apparent molecular weight of 40kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis. In addition, it had fibrinolytic activity by UV spectrophotometry. Optimum pH was 8.0, the optimum temperature was 59℃ and it was stable to heat.The metal ion Na^＋ had little effect to the protein＇ s activity and K^＋ , Mg^2＋ ,Ca^2＋ could increase its activity.The thrombolytic activity on fibrin was measured by fibrin plate method.The results showed the enzyme had strong thrombolytic action on fibrin.
出处
《食品工业科技》
CAS
CSCD
北大核心
2009年第6期76-79,共4页
Science and Technology of Food Industry
基金
国家自然科学基金(30772739)
关键词
福寿螺
纤溶活性蛋白
分离纯化
性质
Ampullarum crossean
fibrinolytic protein
purification
character
