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PMID: 3029775 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Yeung YG, Jubinsky PT, Sengupta A, Yeung DC, Stanley ER

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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25 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1987-03-00
Pages
1268-71
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC304408
Subset
IM
Grants
NCI NIH HHS · CA26504 · United States
NIGMS NIH HHS · GM7288 · United States
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