the results shows that the vitro expressed protein of n gene by recombinant plasmid vector in the e . coli maintains anigenicity of tgev the recombinant protein was purified acconiing to the vector self characteristic ( hisk a polyhishdine tag introduced at the amino-acid terminus of the nucleoprotein allowed for the purification of protein by nickel-chelate dsity chromataography we explored all possibilities of pedcation and gained the modified purification method . several conditions, which include diffend ph buffer and concelltheion of imidazole, were selected to purify recombinan nucleorotein 根据载体pproexhtb含有(his)6特点,将融合蛋白进行纯化,在纯化过程中经各项条件的探索,确定为在裂解液中含有1mmpmsf的条件下,分别经过2倍体积的buffera和bufferb洗脱后,再收集ph5.9,含有80mmol/l咪唑的1倍体积bufferc洗脱液,可得到纯化的融合蛋白。