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从竹叶青蛇中分离并鉴定一种新型P-II类蛇毒金属蛋白酶

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

作者信息

Han Yao-Ping, Lu Xiang-Yun, Wang Xue-Feng, Xu Juan

机构信息

Department of Biology and Food Science, Changshu Institute of Technology, 98 Yuanhe Road, Changshu, Jiangsu 215500, China.

出版信息

Toxicon. 2007 Jun 1;49(7):889-98. doi: 10.1016/j.toxicon.2006.11.030. Epub 2006 Dec 15.

DOI:10.1016/j.toxicon.2006.11.030
PMID:17403531
Abstract

Stejnitin, a novel class P-II snake venom metalloproteinase (SVMP) with a molecular weight of about 35kDa, 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).

摘要

竹叶青素是一种新型的P-II类蛇毒金属蛋白酶(SVMP),分子量约为35kDa,从竹叶青蛇毒中纯化得到。竹叶青素的cDNA编码一个由295个氨基酸残基组成的多肽,其包含信号肽、前体蛋白、金属蛋白酶结构域、间隔区和去整合素结构域。通过肽质量指纹图谱分析证实了从cDNA推导的蛋白质序列。它与同时包含金属蛋白酶和去整合素的P-IIa亚类SVMP成员高度同源。DNA片段化和流式细胞术分析结果还表明,竹叶青素能够诱导ECV304细胞凋亡(R = 0.908,P = 0.012)。

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