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

Y. G. Yeung, P. T. Jubinsky, A. Sengupta, E. R. Stanley

Research output: Contribution to journalArticlepeer-review

58 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1268-1271
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume84
Issue number5
DOIs
StatePublished - 1987

ASJC Scopus subject areas

  • General

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