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- W2352912181 abstract "Objective To construct the prokaryotic expression vector of HSP65-T cell epitopes of MOMP of C. trachomatis (Ct) fusion protein (called H-ctml), express and purify H-ctml. Methods The HSP65 and gene sequence of T cell epitopes of MOMP of Ct (ctml) were obtained by PCR method and cloned into pMD18-T vector respectively. The T vector was digested by endonuclease for releasing the fragment of HSP65 or ctml gene. The gene of HSP65 and ctml were cloned into pET28a plasmid successively to construct the prokaryotic expression vector (pET28a-H-ctml), which recombined the gene of HSP65 and ctml. The E. coli BL21 (DE3) transformed with pET28a-H-ctml were induced by IPTE for expression of H-ctml fusion protein. The protein was purified by Ni2+ affinity chromatography. Results The prokaryotic expression vector, pET28a-H-ctml, was constructed successfully. The fusion protein of H-ctml was expressed in E. coli BL21 (DE3). The purity of fusion protein was 98% after purified by Ni2+ affinity chromatography. Conclusion The prokaryotic expression vector of pET28a-H- ctml has been constructed, and the fusion protein with biological activity has been successfully expressed and purified." @default.
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- W2352912181 date "2006-01-01" @default.
- W2352912181 modified "2023-10-07" @default.
- W2352912181 title "Gene recombinant and prokaryotic expression of HSP65-T cell epitopes of MOMP of C. trachomatis fusion protein and its purification" @default.
- W2352912181 hasPublicationYear "2006" @default.
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