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. 1987 Mar;84(5):1268–1271. doi: 10.1073/pnas.84.5.1268

Purification of the colony-stimulating factor 1 receptor and demonstration of its tyrosine kinase activity.

Y G Yeung, P T Jubinsky, A Sengupta, D C Yeung, E R Stanley
PMCID: PMC304408  PMID: 3029775

Abstract

Colony-stimulating factor 1 (CSF-1) regulates the survival, proliferation, and differentiation of mononuclear phagocytes. The CSF-1 receptor was purified from cell membranes of the J774.2 mouse macrophage cell line by solubilization with Triton X-100, CSF-1 affinity chromatography, and gel filtration. The purified receptor is a protein or glycoprotein of 165 kDa comprising a single polypeptide chain that is not covalently associated, either as a homopolymer, or with any other protein. CSF-1 stimulated autophosphorylation of the purified receptor in tyrosine residues. Casein but not histone was shown to act as a substrate for the tyrosine protein kinase activity of purified receptor.

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Selected References

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