High expression and simultaneous renaturation and purification of the recombinant chicken IFN-α.

The IFN-α gene of chicken was synthesized using optimized codons based on online analysis tools and bio-software and cloned into the pWL expression vector.The recombinant plasmid was transformed into Escherichia coli for expression.SDS-PAGE analysis showed that the expressed protein had a molecular weight of 19ku and accounted for 28.3% of the total cellular protein.The expression product mainly existed in the form of inclusion bodies.The dissolved inclusion body proteins were denatured and renatured simultaneously to purify the chicken IFN-α by gel filtration using Sephadex G50.The purity of the renatured IFN-α was exceed 98%and the yield reached 47.1mg/L(34.14%) and the resultant IFN-α showed a strong antiviral activity of 1.12×108U/mg on CEF/NDV culture.