Synthesis of recombinant gamma interferons resistant to proteolysis in the yeast Pichia pastoris

Genes encoding truncated versions of bovine and chicken gamma interferon genes lacking predicted protease cleavage sites at the C-terminus were constructed and expressed in the yeast Pichia pastoris. The recombinant proteins possessed increased stability in comparison with the corresponding wild-type gamma interferons while retaining biological activity. The recombinant strains provide a useful tool for the purification of bovine and chicken gamma interferons for their use in veterinary applications.