[Expression and purification of recombinant Schistosoma japonicum paramyosin].
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.
Zhou
J C
JC
Department of Parasitology, Hunan Medical University, Changsha 410078.
Yi
X Y
XY
Kalinna
B H
BH
McManus
D P
DP
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*
D000947:Antigens, Helminth; D011994:Recombinant Proteins; D014335:Tropomyosin