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. 1985 Oct;4(10):2575–2581. doi: 10.1002/j.1460-2075.1985.tb03973.x

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

J F DeLamarter, J J Mermod, C M Liang, J F Eliason, D R Thatcher
PMCID: PMC554546  PMID: 3902470

Abstract

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.

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