Biochemical properties of the 75-kDa tumor necrosis factor receptor. Characterization of ligand binding, internalization, and receptor phosphorylation.

@article{Pennica1992BiochemicalPO,
  title={Biochemical properties of the 75-kDa tumor necrosis factor receptor. Characterization of ligand binding, internalization, and receptor phosphorylation.},
  author={Diane Pennica and Vu Tung Lam and Nancy K. Mize and Rosina. Weber and Matthew C Lewis and Brian M. Fendly and Michael T. Lipari and David V. Goeddel},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 29},
  pages={21172-8}
}
An expression plasmid encoding the human 75-kDa tumor necrosis factor (TNF) type 2 receptor (TNF-R2) was constructed and used to generate a stable human cell line (293/TNF-R2) overexpressing TNF-R2. Ligand binding analysis revealed high affinity binding (Kd = 0.2 nM) with approximately 94,000 +/- 7,500 sites/cell for 125I-TNF-alpha and approximately 5-fold lower affinity for TNF-beta (Kd = 1.1 nM) with 264,000 +/- 2,000 sites/cell. Cross-linking of 125I-TNF-alpha and 125I-TNF-beta to 293/TNF-R2… CONTINUE READING

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