Isolation and in vitro partial characterization of hemolytic proteins from the nematocyst venom of the jellyfish Stomolophus meleagris

被引:29
|
作者
Li, Rongfeng [1 ]
Yu, Huahua [1 ]
Xing, Ronge [1 ]
Liu, Song [1 ]
Qing, Yukun [1 ]
Li, Kecheng [1 ,2 ]
Li, Bing [1 ,2 ]
Meng, Xiangtao [1 ,2 ]
Cui, Jinhui [1 ,2 ]
Li, Pengcheng [1 ]
机构
[1] Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China
[2] Grad Univ, Chinese Acad Sci, Beijing 100039, Peoples R China
基金
中国国家自然科学基金;
关键词
Jellyfish Stomolophus meleagris; Nematocyst venom; Isolation; Hemolysis; SmTX; RHOPILEMA-ESCULENTUM KISHINOUYE; CYANEA-NOZAKII KISHINOUYE; BOX JELLYFISH; PARTIAL-PURIFICATION; SEA WASP; CARYBDEA-MARSUPIALIS; CHIRONEX-FLECKERI; TOXIN; BINDING; ALATA;
D O I
10.1016/j.tiv.2013.04.004
中图分类号
R99 [毒物学(毒理学)];
学科分类号
100405 ;
摘要
Jellyfish venom contains various toxins and can cause itching, edema, muscle aches, shortness of breath, blood pressure depression, shock or even death after being stung. Hemolytic protein is one of the most hazardous components in the venom. The present study investigated the hemolytic activity of the nematocyst venom from jellyfish Stomolophus meleagris. Anion exchange chromatography, DEAE Sepharose Fast Flow, and gel filtration chromatography, Superdex200 had been employed to isolate hemolytic proteins from the nematocyst venom of jellyfish S. meleagris. Hemolysis of chicken red blood cells was used to quantify hemolytic potency of crude nematocyst venom and chromatography fractions during the purification process. Native-PAGE profile displayed one protein band in the purified hemolytic protein (SmTX); however, two protein bands with apparent molecular weights of similar to 45 kDa and 52 kDa were observed in the reducing SDS-PAGE analysis. Approximately 70 mu g/mL of SmTX caused 50% hemolysis (HU50) of the erythrocyte suspension. The hemolytic activity of SmTX was shown to be temperature and pH dependent, with the optimum temperature and pH being 37 degrees C and pH 5.0. The present study is the first report of isolation and partial characterization of hemolytic proteins from the nematocyst venom of the jellyfish S. meleagris. The mechanism of the hemolytic activity of SmTX is not clear and deserves further investigation. (C) 2013 Published by Elsevier Ltd.
引用
收藏
页码:1620 / 1625
页数:6
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