Expression and characterization of Kringle 1-4.5 domains of human plasminogen | |
Zhou, QW; Xie, JL; Xin, L; Xu, R; Ye, Q; Li, ZP; Gan, RB | |
刊名 | ACTA BIOCHIMICA ET BIOPHYSICA SINICA |
2003 | |
卷号 | 35期号:2页码:138-142 |
关键词 | K1-4. 5 Pichia pastoris expression purification bioactivity |
通讯作者 | , |
英文摘要 | The cDNA encoding Kringle 1-4 and part of Kringle 5 domains of human plasminogen (K1-4.5), obtained from HepG2 by RT-PCR, was cloned into expression vector pHIL-SI. The recombinant plasmid pHIL-K 1-4. 5 was transformed into Pichia pastoris GS115 and the recombinant yeast was induced to express the recombinant proteins by methanol. The expressed proteins were purified by lysine affinity chromatography to a purity of 95%. The recombinant K 1-4. 5 inhibited the growth of bovine capillary endothelial cells ( BAEC) stimulated by the basic fibroblast growth factor ( bFGF), in a dosage-dependent manner with a half maximal concentration of 2 mg/L. rhKl-4.5 also inhibited 40% of the BAEC migration stimulated by bFGF in the concentration of I mg/L. |
学科主题 | Biochemistry & Molecular Biology; Biophysics |
类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
关键词[WOS] | PICHIA-PASTORIS ; HUMAN ANGIOSTATIN ; GROWTH-FACTOR ; ANGIOGENESIS ; INHIBITOR ; SUPPRESSION ; CANCER |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000181245500007 |
内容类型 | 期刊论文 |
版本 | 出版稿 |
源URL | [http://202.127.25.143/handle/331003/2253] |
专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
推荐引用方式 GB/T 7714 | Zhou, QW,Xie, JL,Xin, L,et al. Expression and characterization of Kringle 1-4.5 domains of human plasminogen[J]. ACTA BIOCHIMICA ET BIOPHYSICA SINICA,2003,35(2):138-142. |
APA | Zhou, QW.,Xie, JL.,Xin, L.,Xu, R.,Ye, Q.,...&Gan, RB.(2003).Expression and characterization of Kringle 1-4.5 domains of human plasminogen.ACTA BIOCHIMICA ET BIOPHYSICA SINICA,35(2),138-142. |
MLA | Zhou, QW,et al."Expression and characterization of Kringle 1-4.5 domains of human plasminogen".ACTA BIOCHIMICA ET BIOPHYSICA SINICA 35.2(2003):138-142. |
个性服务 |
查看访问统计 |
相关权益政策 |
暂无数据 |
收藏/分享 |
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。
修改评论