A major binding protein for leukemia inhibitory factor in normal mouse serum: identification as a soluble form of the cellular receptor.

@article{Layton1992AMB,
  title={A major binding protein for leukemia inhibitory factor in normal mouse serum: identification as a soluble form of the cellular receptor.},
  author={Meredith J. Layton and Belinda Cross and Donald Metcalf and Larry D Ward and Richard J. Simpson and Nicos A. Nicola},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1992},
  volume={89 18},
  pages={8616-20}
}
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… CONTINUE READING

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