Study on the expression,purification and bioactivity of recombinant T?16 / 中国免疫学杂志

ABSTRACT

Objective:To study the bioactivity of thymosin ?16 (T?16) in vitro and in vivo.Methods:Recombinant His-SUMO-T?16 was constructed and transformed into E.coli BL21(DE3) for induced expression.The product was treated by ultrasonication,ion-exchange chromatography and metal chelation chromatography respectively for purification.The fusion protein was cut by His-SUMO protease and then further purified by metal chelation chromatography and Superdex 30 gel chromatography.Results:Recombinant fusion protein His-SUMO-T?16 was soluble,whose specific activity was 5.3?105 U/mg.It could promote the proliferation of BALB/c 3T3 cells,rabbit corneal cells,and chicken embryo chorion vessels in vitro,and both the proliferation and migration of vascular endothelial cells in vitro were enhanced,and rabbit skin healing of alkali burns in vivo was accelerated.Conclusion:E.coli expressing vector of recombinant His-SUMO-T?16 fusion protein is constructed successfully,and recombinant protein T?16 has significant repairing effects.The study established a good foundation for further industrialization of T?16.