Abstract:
:A protein that specifically binds leukemia inhibitory factor (LIF) has been isolated from normal mouse serum by using four successive fractionation steps: chromatography on a LIF affinity matrix, anion-exchange chromatography, size-exclusion chromatography, and preparative native gel electrophoresis. The purified LIF-binding protein (LBP) is a glycoprotein with an apparent molecular mass of 90 kDa that specifically binds 125I-labeled murine LIF with an affinity comparable to that of the low-affinity cellular LIF receptor (Kd = 600 pM). N-terminal sequencing has identified this protein as a soluble truncated form of the alpha chain of the cellular LIF receptor. LBP is present in normal mouse serum at high levels (1 microgram/ml) and these levels are elevated in pregnant mice and reduced in neonatal mice. Since normal serum concentrations of LBP can block the biological actions of LIF in culture, LBP may serve as an inhibitor of the systemic effects of locally produced LIF.
journal_name
Proc Natl Acad Sci U S Aauthors
Layton MJ,Cross BA,Metcalf D,Ward LD,Simpson RJ,Nicola NAdoi
10.1073/pnas.89.18.8616keywords:
subject
Has Abstractpub_date
1992-09-15 00:00:00pages
8616-20issue
18eissn
0027-8424issn
1091-6490journal_volume
89pub_type
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