福寿螺纤溶活性蛋白的纯化及性质研究  

Purification and biochemical character of a fibrinolytic protein from Ampullarum crossean

作　　者：陈明军[1] 谭竹钧[1] 刘兵[1] 李穗晶[1] 张冬梅[1] 

机构地区：[1]广东工业大学轻工化工学院,广东广州510006

出　　处：《食品工业科技》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)

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.

关 键 词：福寿螺 纤溶活性蛋白 分离纯化 性质 

分 类 号：TS254.1[轻工技术与工程—水产品加工及贮藏工程]