单环刺螠纤溶酶UFE-Ⅰ的性质和溶栓活性  

Characterization and Thrombolysis Activity of Fibrinolytic Enzyme UFE-I from Urechis unicinctus

作　　者：初金鑫[1,2] 蔡文娣[1,2] 韩宝芹[2] 刘万顺[2] 陈丽梅[1] 连波[1] 

机构地区：[1]潍坊医学院基础医学教学部,潍坊261053 [2]中国海洋大学海洋生命学院,青岛266003

出　　处：《天然产物研究与开发》2010年第4期661-664,共4页Natural Product Research and Development

摘　　要：单环刺螠纤溶酶UFE-Ⅰ的最适反应温度为45℃;最适反应pH为7.0;Mg2+、Mn2+和Fe2+是该纤溶酶的强激活剂;Fe3+、Cu2+、Ag+、Hg+和Pb2+对该纤溶酶具有一定的抑制作用;SBTI和PMSF,完全抑制UFE-Ⅰ,说明该酶为丝氨酸蛋白酶;糜蛋白酶抑制剂部分抑制UFE-Ⅰ,亮抑酶肽、抑蛋白酶肽、苯甲脒较弱的抑制UFE-Ⅰ。与蚓激酶类似,UFE-Ⅰ不仅具有直接的纤溶活力更具有纤溶酶原激活活力(84.0%),另外分别将蚓激酶原料与该酶加入到家兔血栓块中,37℃孵育3 h,结果表明该酶具有比蚓激酶更为强大的溶栓能力。The optimum temperature of UFE-Ⅰ was about 45 ℃.The optimum pH was about 7.0.It was discovered that Fe3＋、Cu2＋、Ag＋、Hg＋ and Pb2＋ ions were inhibitors of UFE-Ⅰ,and Mg2＋、Mn2＋ and Fe2＋ ions were activators of this enzyme.SBTI（soybean trypsin inhibitor） and PMSF（phenylmethyl sulfonylfluoride） completely inhibited UFE-Ⅰ,which indicated that the enzyme belonged to serine protease group,chymotrypsin inhibitor fractionaly inhibited UFE-Ⅰ,leupeptin、aprotinin and benzamidine inhibited UFE-Ⅰweakly.Like lumbrokinase,UFE-Ⅰ can not only directly degrade fibrin but also indirectly hydrolyze fibrin through transforming plasminogen into plasmin（84.0%）.when each enzyme and rabbit thrombus was incubated at 37 ℃ for 3 h.The results showed that UFE-Ⅰhad stronger thrombolytic ability than lumbrokinase.

关 键 词：单环刺螠 纤溶酶 性质 溶栓活性 

分 类 号：Q503[生物学—生物化学]