真菌来源的新的纤溶蛋白  

A Novel Fibrinolytic Protein from Fungi

作　　者：吴黎诚[1] 吴斌[2] 夏焕章[1] 陈代杰[2] 戈梅[3] 

机构地区：[1]沈阳药科大学生命科学与生物制药学院,辽宁沈阳110016 [2]上海医药工业研究院,上海200040 [3]上海来益生物药物研发中心,上海201203

出　　处：《药物生物技术》2008年第5期365-369,共5页Pharmaceutical Biotechnology

基　　金：国家资源平台项目;<药用微生物资源标准资源整理;整合及共享试点项目>;项目编号2005DKA21203

摘　　要：本文研究了一种新的纤溶活性蛋白,并对其产生菌(植物内生真菌CPCC 480097)进行了鉴定。经形态学观察和ITS序列分析,CPCC 480097为镰孢霉属(Fusariumsp.)。该菌的发酵液经离心、盐析、Mono-Q阴离子交换和Superdex 75凝胶过滤,获得电泳纯的纤溶蛋白Fu-P,相对分子质量约为28 k。最终纯化倍数和收率分别为158.5倍和6.8%,其相对于尿激酶的比活为76 111 U/mg。Fu-P的N-端15个氨基酸序列为QASSGTPATIRVLVV,与已报道的其它微生物所产的纤溶酶有较大的差异。Fungi CPCC 480097, which produced a fibrinolytic protein （Fu-P） were identified as Fusarium sp. by the morphological and ITS sequence analysis. Fu-P was purified from the supernatant of CPCC 480097 culture broth by 40%- 60% ammonium sulfate precipitation, ion-exchange chromatography on Mono Q, and gel filtration on Superdex 75. The purified protein was analyzed with SDS-PAGE. The protein was a 28 k single chain protein with an isoelectric point of 8. 1. The purification factor and activity recovery of the fibrinolytic protein were 158.5 fold and 6.8% respectively. The first 15 amino acids of the N terminal sequence of Fu-P were QASSGTPATIRVLVV, which were different from those fihrinolytic enzymes produced by other micro-organisms.

关 键 词：镰孢霉属 纤溶 鉴定 分离纯化 

分 类 号：Q51[生物学—生物化学]