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.
MeSH Terms
Animals
Cell Line
Colony-Stimulating Factors/metabolism
Kinetics
Macrophages
Mice
Molecular Weight
Phosphorylation
Protein-Tyrosine Kinases/metabolism
Receptors, Cell Surface/isolation & purification,metabolism
Receptors, Colony-Stimulating Factor
Chemicals
Colony-Stimulating Factors
Receptors, Cell Surface
Receptors, Colony-Stimulating Factor
Protein-Tyrosine Kinases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Yeung Y G
Jubinsky P T
Sengupta A
Yeung D C
Stanley E R
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