Abstract: Gene fragment argR from Corynebacterium crenatum was amplified by PCR and inserted into pET22b(+) vector to construct a recombinant plasmid pET22b-argR. The recombinant plasmid pET22b-argR was transformed into E. coli BL21(DE3) for protein expression. The protein ArgR with molecular weight of 20 kD was successfully expressed in E. coli BL21(DE3)under the induction of IPTG at 33 ℃ for 8 h. The ArgR fusion protein was purified by Ni2+ affinity column chromatography for preparing polyclonal antibody. ELISA analysis showed that the antibody titer was 1:160000. Western blot analysis revealed that the antibody could react specifically with the expressed recombinant protein and that the purified ArgR was stable in the form of polymer mediated by L-arginine. These investigations can provide a theoretical reference for detecting the interaction between ArgR and promoters from arginine biosynthetic pathway of C. crenatum.

Key words: C. crenatum, argR gene, high-level expression, affinity purification, polymer