Recombinant murine GM-CSF from E. coli has biological activity and is neutralized by a specific antiserum.

We report the production and characterization of a mouse granulocyte-macrophage colony stimulating factor (mGM-CSF) made in Escherichia coli. The synthesis of mGM-CSF was directed by a plasmid containing a gene isolated from the EL-4 cell line. After induction of expression and accumulation of the protein in E. coli, mGM-CSF accounted for 10% of total cellular protein. This recombinant mGM-CSF was purified to 90% homogeneity by chaotrope extraction and gel filtration. Recombinant mGM-CSF, like the native molecule, stimulates the growth of granulocyte and macrophage colonies in serum-free cultures of mouse bone marrow cells. Antibodies raised against recombinant mGM-CSF not only reacted with the recombinant protein but also neutralized the biological activity of both native and recombinant mGM-CSF. These results indicate that the functional structure of the recombinant protein is similar to that of native mGM-CSF.