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Two-step purification and in vitro characterization of a hemolysin from the venom of jellyfish Cyanea nozakii Kishinouye
Li, Rongfeng1,2; Yu, Huahua1; Feng, Jinhua1; Xing, Ronge1; Liu, Song1; Wang, Lin1,2; Qin, Yukun1,2; Li, Kecheng1,2; Li, Pengcheng1
2011-07-01
发表期刊INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
ISSN0141-8130
卷号49期号:1页码:14-19
文章类型Article
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.
关键词Jellyfish Cyanea Nozakii Kishinouye Hemolysis Venom
学科领域Biochemistry & Molecular Biology
DOI10.1016/j.ijbiomac.2011.03.005
URL查看原文
收录类别SCI
语种英语
WOS记录号WOS:000291840400003
引用统计
被引频次:16[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.qdio.ac.cn/handle/337002/12057
专题海洋生物技术研发中心
实验海洋生物学重点实验室
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
第一作者单位中国科学院海洋研究所
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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.
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