Single-step Purification and Refolding of Recombinant Human Angiogensis Inhibitor(rhB)

The gene expression product rhB existed in E.Coli in inclusion bodies. The recombinant protein was yurified under denaturing conditions with affinity of 6 histidine residues at its N-terminal to metal chelate chromographic matrixes. The experimential results showed that the purified recombinant protein under denaturing conditions was immediately refolded in Ni-NTA column using 8.0mol/L～1.0mol/L urea at a linear gradient. The method effectuvely improved the protein renature, which is simple,rapid and efficient. High pure and active recombinant protein was ontained by the single-step method.