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一种来自海洋细菌的血纤维蛋白溶酶的分离纯化及性质研究
引用本文:魏香,刘晨光,刘万顺,刘成圣,韩宝芹.一种来自海洋细菌的血纤维蛋白溶酶的分离纯化及性质研究[J].海洋科学,2001,25(3):1-4.
作者姓名:魏香  刘晨光  刘万顺  刘成圣  韩宝芹
作者单位:青岛海洋大学生命学院生化室
基金项目:国家海洋863青年基金!资助项目819 Q 10号
摘    要:利用硫酸铵分级盐析、DEAE-纤维素阴离子交换层析、Sephadex G-75凝胶层析法对由海洋细菌FE92-8分泌的纤维蛋白溶酶进行了分离纯化,结果得到SDS-聚丙烯酰胺凝胶电泳单一区带。性质研究发现,该酶分子量为12.6kD,等电点为7.45,琼脂糖-纤维蛋白平板法测得该酶作用的最适温度为50℃,最适pH为8.0,在37℃,pH为8.0的情况下表现出很好的稳定性,温度起来50℃热稳定性较差,在碱性环境中稳定性较在酸性环境中稳定性强,阴性平板和阳性平板对比实验发现,该酶只有纤溶活性而无激酶活性,体外实验发现,该酶具有快速溶解血栓的能力。

关 键 词:血纤维蛋白溶酶  分离纯化  性质  海洋细菌
收稿时间:2000/10/30 0:00:00
修稿时间:2000年10月30

PURIFICATION AND PROPERTY OF A PLASMIN FROM A MARINE BACTERIA
WEI Xiang, LIU Chen-guang LIU Wan-shun HIU Cheng-sheng HAN Bao-qin.PURIFICATION AND PROPERTY OF A PLASMIN FROM A MARINE BACTERIA[J].Marine Sciences,2001,25(3):1-4.
Authors:WEI Xiang  LIU Chen-guang LIU Wan-shun HIU Cheng-sheng HAN Bao-qin
Institution:WEI Xiang1,2 LIU Chen-guang1 LIU Wan-shun1 HIU Cheng-sheng1 HAN Bao-qin1
Abstract:The plasmin was purified from the fermentation solution by using of ammonium sulfate precipitation, DEAD-cellulose ion-exchange column chromatography and Sephadex G-75 gel filtration column chromatography. The purified enzyme showed a single band on PAGE and a level of fibrinolysis activity about 5.16 times that of the crude enzyme. The molecular weight was 12.6 kD determined by SDSげ PAGE. The isoげ electric point(pI) was proved to be 7.45 by fast polyacrylamide isoげ electric focus electrophoresis. The fibrinolysis activity was determined by aragoseげ fibrous protein plate method. The optimum temperature and pH were 50 → and 8.0 respectively. It is stable in the basic solution. According to the control of activity of this enzyme between positive and negative plate, this enzyme had high affinity to fibrin, and the ability of activating plasminogen was low. In vitro, this enzyme had strong ability to hydrolyze artificial thrombus.
Keywords:Plasmin  Isolate and purify  Different property  
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