4.5 Article

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

Journal

TOXICOLOGY IN VITRO
Volume 27, Issue 6, Pages 1620-1625

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.tiv.2013.04.004

Keywords

Jellyfish Stomolophus meleagris; Nematocyst venom; Isolation; Hemolysis; SmTX

Categories

Funding

  1. National Natural Science Foundation of China [41006095]
  2. National Key Technologies RD Program [2011BAE06B04]
  3. Knowledge Innovation Program of the Chinese Academy of Sciences [KZC-YW-205-03]

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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.

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