Fusion Expression of Recombinant Human Nerve Growth Factor β-Subunit in Escherichia coli and Their Activity Assay

Objective:To acquire recombinant human nerve growth factor(rhNGF) β-subunit with the biological activity similar to that native protein in E.coli. Methods:The β-subunit of rhNGF was expressed in E.coli fused with DsbA,DsbC or Trx protein. After optimizing renature condition,we got three soluble rhNGF fusion proteins and further examined their biological activities by the biological assay on dorsal root ganglia from chicken embryos. Results:Among the three fusion proteins,only DsbA-L-NGF has the activity similar to native mouse NGF which can promote chicken diosal root ganglia to form outgrowth. Conclusion:rhNGF β-subunit would display good biological activity when it was fusion expressed with DsbA in E.coli.