Two-step purification and in vitro characterization of a hemolysin from the venom of jellyfish Cyanea nozakii Kishinouye

doi:10.1016/j.ijbiomac.2011.03.005

	Two-step purification and in vitro characterization of a hemolysin from the venom of jellyfish Cyanea nozakii Kishinouye
	Li, Rongfeng 1,2; Yu, Huahua1 ; Feng, Jinhua 1; Xing, Ronge1 ; Liu, Song 1; Wang, Lin1,2 ; Qin, Yukun 1,2; Li, Kecheng 1,2; Li, Pengcheng1
刊名	INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
	2011-07-01
卷号	49 期号:1 页码:14-19
关键词	Jellyfish Cyanea Nozakii Kishinouye Hemolysis Venom
ISSN号	0141-8130
DOI	10.1016/j.ijbiomac.2011.03.005
文献子类	Article
英文摘要	Hemolysin is one of the most hazardous components in the venom of Cyanea nozakii Kishinouye. Here we describe the purification and in vitro characterization of the hemolysin, which we named CnPH. The CnPH was isolated by anion-exchange and size-exclusion chromatography from the nematocyst venom. Two protein bands with molecular masses of 20 kDa, 60 kDa respectively were shown in the reducing SOS-PAGE analysis of the CnPH. And Approximately 5 mu g/mL of the CnPH resulted in 50% hemolysis of the erythrocyte suspension. The hemolytic activity of the CnPH was both temperature and pH dependent. Moreover, it was significantly inhibited in the presence of divalent metal cations, including Cu(2+), Mg(2+), Mn(2+), Zn(2+) and Ca(2+), but enhanced in the presence of EDTA. However, how CnPH performs its hemolytic activity is not yet clear, therefore the mechanism of the hemolytic activity of the CnPH is under research. (C) 2011 Elsevier B.V. All rights reserved.; Hemolysin is one of the most hazardous components in the venom of Cyanea nozakii Kishinouye. Here we describe the purification and in vitro characterization of the hemolysin, which we named CnPH. The CnPH was isolated by anion-exchange and size-exclusion chromatography from the nematocyst venom. Two protein bands with molecular masses of 20 kDa, 60 kDa respectively were shown in the reducing SOS-PAGE analysis of the CnPH. And Approximately 5 mu g/mL of the CnPH resulted in 50% hemolysis of the erythrocyte suspension. The hemolytic activity of the CnPH was both temperature and pH dependent. Moreover, it was significantly inhibited in the presence of divalent metal cations, including Cu(2+), Mg(2+), Mn(2+), Zn(2+) and Ca(2+), but enhanced in the presence of EDTA. However, how CnPH performs its hemolytic activity is not yet clear, therefore the mechanism of the hemolytic activity of the CnPH is under research. (C) 2011 Elsevier B.V. All rights reserved.
学科主题	Biochemistry & Molecular Biology
URL标识	查看原文
语种	英语
WOS记录号	WOS:000291840400003
公开日期	2012-07-03
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/12058]
专题	海洋研究所_海洋生物技术研发中心海洋研究所_实验海洋生物学重点实验室海洋研究所_海洋环境工程技术研究发展中心
作者单位	1.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100039, Peoples R China
推荐引用方式 GB/T 7714	Li, Rongfeng,Yu, Huahua,Feng, Jinhua,et al. Two-step purification and in vitro characterization of a hemolysin from the venom of jellyfish Cyanea nozakii Kishinouye[J]. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,2011,49(1):14-19.
APA	Li, Rongfeng.,Yu, Huahua.,Feng, Jinhua.,Xing, Ronge.,Liu, Song.,...&Li, Pengcheng.(2011).Two-step purification and in vitro characterization of a hemolysin from the venom of jellyfish Cyanea nozakii Kishinouye.INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,49(1),14-19.
MLA	Li, Rongfeng,et al."Two-step purification and in vitro characterization of a hemolysin from the venom of jellyfish Cyanea nozakii Kishinouye".INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 49.1(2011):14-19.