Authors : Chien C. Loa , Ming K. Hsieh , Ching C. Wu and Tsang L. Lin
Abstract: The turkey interferon gamma (IFN- ) protein was expressed in a prokaryotic expression system as histidine-tagged fusion protein and functional activity of the recombinant protein was examined. The turkey IFN- gene was subcloned from a recombinant pCR3.1-IFN construct to the prokaryotic expression vector pQE30. The recombinant expression construct (pQE-IFN ) was identified by polymerase chain reaction and sequencing analysis. Expression of histidine-tagged fusion protein with molecular mass of 23 - 24 kd was determined by Western blotting analysis with monoclonal antibodies specific to the histidine-tag or chicken IFN- . The protein recovery was 7 mg from 500 ml of bacterial culture. The purified recombinant protein was capable of activating macrophage and inducing production of nitric oxide. The functional activity of the recombinant protein could be neutralized by a monoclonal antibody specific to chicken IFN- . These results indicated that the expressed protein was a biologically functional turkey IFN- protein.
Chien C. Loa , Ming K. Hsieh , Ching C. Wu and Tsang L. Lin , 2003. Expression and Functional Characterization of Recombinant Turkey IFN-r . Journal of Animal and Veterinary Advances, 2: 648-653.