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Isolation and Identification of Heat Shock Protein 60(Hsp60) from the Nematocyst of Jellyfish Cyanea nozakii Kishinouye |
LI Rong-feng1,2, YU Hua-hua1, XING Rong-e1, LIU Song1, LI Peng-cheng1 |
1. Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China;
2. Graduate University of the Chinese Academy of Sciences, Beijing 100039, China |
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Abstract Heat shock protein 60 (Hsp60), an important member of the molecular chaperonin family, plays significant roles in the transportation, assembly and folding. Here, a fast method of the purification of Hsp60 from the nematocyst of jellyfish Cyanea nozakii Kishinouye was described. The Hsp60 was achieved by a two-step separation of anion-exchange and size-exclusion chromatography. Subsequently, SDS-PAGE analysis revealed that the purified protein was an apparent and single protein band with a molecular mass of 60 kDa and the N-terminal amino acid sequences of APKEIKFGADAKSLM, which is accordance with the sequences of heat shock protein 60 and its identity was also confirmed by a highly sensitive sandwich ELISA, which is used to quantitate Hsp60 levels of the crude and isolated protein. The method of the purification of Hsp60 from the jellyfish Cyanea nozakii Kishinouye is very helpful to the study of the potential functions and further application of Hsp60.
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Received: 24 June 2011
Published: 25 October 2011
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