Isolation and characterization of a novel P-II class snake venom metalloproteinase from Trimeresurus stejnegeri

被引：23

作者：

Han, Yao-Ping ^{[1
]}

Lu, Xiang-Yun ^{[1
]}

Wang, Xue-Feng ^{[1
]}

Xu, Juan ^{[1
]}

机构：

[1] Changshu Inst Technol, Dept Biol & Food Sci, Changshu 215500, Jiangsu, Peoples R China

来源：

TOXICON | 2007年 / 49卷 / 07期

关键词：

apoptosis; ECV304; cell; metalloproteinase; snake venom; FUNCTIONAL-CHARACTERIZATION; MOLECULAR-CLONING; CDNA CLONING; DISINTEGRIN; APOPTOSIS; PURIFICATION; PROTEIN; ECV304; EXPRESSION; MEMBERS;

D O I：

10.1016/j.toxicon.2006.11.030

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

Stejnitin, a novel class P-II snake venom metalloproteinase (SVMP) with a molecular weight of about 35 kDa, was purified from Trimeresurus stejnegeri venom. The cDNA of stejnitin encoded a polypeptide of 295 amino acid residues which comprises a signal peptide, proprotein, metalloproteinase domain, spacer and disintegrin domain. The protein sequence deduced from cDNA was confirmed by peptide mass fingerprinting analysis. It is highly homologous to the members of subclass P-IIa SVMPs which comprises metalloproteinase and disintegrin together. Results from DNA fragmentation and flow cytometry analysis also indicated that stejnitin is able to induce apoptosis of ECV304 cells (R=0.908, P=0.012). © 2007 Elsevier Ltd. All rights reserved.

引用

页码：889 / 898

页数：10

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