Expression, purification and characterization of recombinant Jerdonitin, a P-II class snake venom metalloproteinase comprising metalloproteinase and disintegrin domains

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	Expression, purification and characterization of recombinant Jerdonitin, a P-II class snake venom metalloproteinase comprising metalloproteinase and disintegrin domains
	Zhu LL 1,2; Yuan C 1,2; Chen Z 1,2; Wang WY2,3; Huang MD1,2; wangwy@mail.kiz.ac.cn ; mhuang@fjirsm.ac.cn
	2010
发表期刊	TOXICON
ISSN	0041-0101
卷号	55 期号:37655 页码:375-380
合作性质	其它
摘要	Jerdonitin is a P-II class snake venom metalloproteinase comprising metalloproteinase and disintegrin domains. In this study, we established a high-level expression system in Pichia pastoris and developed a purification strategy for the recombinant Jerdonitin. This recombinant Jerdonitin degraded fibrinogen at a level of activity comparable with its wild type. The effects of recombinant Jerdonitin on inhibiting ADP-induced human platelet aggregation were in a dose-dependent manner with an IC50 of 248 nM. In addition, we reported here that Jerdonitin can significantly inhibit the growth of several cell lines, including human liver cancer cells (Bel7402), human leukemia cells (K562) and human gastric carcinoma cells (BGC823). This study offers recombinant Jerdonitin that will be valuable for further functional and structural studies of Jerdonitin.
关键词	Jerdonitin Recombinant Protein Expression Snake Venom Metalloproteinases
资助者	Our research was supported by grants from CAS (KSCX2- YW-R-082), Fujian NSF (2009I0029), NSFC (30625011, 30811130467, 30770429) and MOST (2007CB914304 and 2006AA02A313). ; Our research was supported by grants from CAS (KSCX2- YW-R-082), Fujian NSF (2009I0029), NSFC (30625011, 30811130467, 30770429) and MOST (2007CB914304 and 2006AA02A313). ; Our research was supported by grants from CAS (KSCX2- YW-R-082), Fujian NSF (2009I0029), NSFC (30625011, 30811130467, 30770429) and MOST (2007CB914304 and 2006AA02A313). ; Our research was supported by grants from CAS (KSCX2- YW-R-082), Fujian NSF (2009I0029), NSFC (30625011, 30811130467, 30770429) and MOST (2007CB914304 and 2006AA02A313).
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收录类别	其他
资助者	Our research was supported by grants from CAS (KSCX2- YW-R-082), Fujian NSF (2009I0029), NSFC (30625011, 30811130467, 30770429) and MOST (2007CB914304 and 2006AA02A313). ; Our research was supported by grants from CAS (KSCX2- YW-R-082), Fujian NSF (2009I0029), NSFC (30625011, 30811130467, 30770429) and MOST (2007CB914304 and 2006AA02A313). ; Our research was supported by grants from CAS (KSCX2- YW-R-082), Fujian NSF (2009I0029), NSFC (30625011, 30811130467, 30770429) and MOST (2007CB914304 and 2006AA02A313). ; Our research was supported by grants from CAS (KSCX2- YW-R-082), Fujian NSF (2009I0029), NSFC (30625011, 30811130467, 30770429) and MOST (2007CB914304 and 2006AA02A313).
文献类型	期刊论文
条目标识符	http://ir.kiz.ac.cn/handle/152453/5395
专题	其他
通讯作者	wangwy@mail.kiz.ac.cn; mhuang@fjirsm.ac.cn
作者单位	1.State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, 155 Yang Qiao Xi Lu, Fuzhou, Fujian 350002, China 2.Graduate School of Chinese Academy of Sciences, Chinese Academy of Sciences, Beijing 10039, China 3.Department of Animal Toxinology, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, China
推荐引用方式 GB/T 7714	Zhu LL,Yuan C,Chen Z,et al. Expression, purification and characterization of recombinant Jerdonitin, a P-II class snake venom metalloproteinase comprising metalloproteinase and disintegrin domains[J]. TOXICON,2010,55(37655):375-380.
APA	Zhu LL.,Yuan C.,Chen Z.,Wang WY.,Huang MD.,...&mhuang@fjirsm.ac.cn.(2010).Expression, purification and characterization of recombinant Jerdonitin, a P-II class snake venom metalloproteinase comprising metalloproteinase and disintegrin domains.TOXICON,55(37655),375-380.
MLA	Zhu LL,et al."Expression, purification and characterization of recombinant Jerdonitin, a P-II class snake venom metalloproteinase comprising metalloproteinase and disintegrin domains".TOXICON 55.37655(2010):375-380.

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