Expression and purification of recombinant Schistosoma japonicum paramyosin
Zhou, J.C.; Yi, X.Y.; Kalinna, B.H.; McManus, D.P.
Hunan Yi Ke da Xue Xue Bao 25(2): 106-108
2000
ISSN/ISBN: 1000-5625 PMID: 12212189 Document Number: 525034
Paramyosin of Schistosoma japonicum was expressed at a high level in E. coli. The recombinant protein could be easily purified from bacteria lysate by fast protein liquid chromatography(FLPC) on a TALON resin column, due to the protein being expressed with a tag of six histidine residue fused to the N-terminus. The protein was completely soluble and could be eluted under non-denaturing condition using imidazole. To eliminate imidazole and residue of E. coli, the elution was further purified by ion-exchange chromatography. The purified protein will be used in water buffaloes in the study on protective immunity against Schistosoma japonicum.