title: [Expression and purification of recombinant Schistosoma japonicum paramyosin].
abstract: 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.
authors.affiliation: Department of Parasitology, Hunan Medical University, Changsha 410078.
authors.forename: J C
authors.initials: JC
authors.lastname: Zhou
authors.forename: X Y
authors.initials: XY
authors.lastname: Yi
authors.forename: B H
authors.initials: BH
authors.lastname: Kalinna
authors.forename: D P
authors.initials: DP
authors.lastname: McManus
mesh_terms: D000818:Animals; D000947:Antigens, Helminth / Q000096:biosynthesis / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics; D012549:Schistosoma japonicum / Q000235:genetics* / Q000378:metabolism; D014335:Tropomyosin / Q000096:biosynthesis / Q000235:genetics*
chemical_list: D000947:Antigens, Helminth; D011994:Recombinant Proteins; D014335:Tropomyosin