To construct the prokaryotic expression vector of myostatin by genetic engineering technology, the synthesized C-terminal domain (330bp) of myostatin was cloned into the expression vector pQE30 to construct the recombinant plasmids pQE-Ms. The recombinant plasmids pQE-Ms were infected with E.coli DH5α and the recombinant myostatin proteins was expressed in E.coli and identified by Western Blot. The proteins was purified by Ni ion affinity chromatography. The Resultls show that the prokaryotic expression vector of myostatin pQE-Ms was contructed successfully through the restriction analysis and sequencing. The expressed recombinant proteins in E.coli was consistent with myostatin molecular weight by SDS-PAGE and Western Blot identification. The high purity of myostatin protein was attained by purification with Ni ion affinity chromatography. The study of the construction of prokaryotic expression vector of myostatin and purification of myostain would provide an experimental ground in the field of sports medicine such as the detection of myostatin and the further study of special antibody.

Myostatin; pQE30; prokaryotic expression; protein purification