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Bioscience, Biotechnology, and Biochemistry Volume 62, 1998 - Issue 9
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Original Articles

Expression and Purification of Cytokine Receptor Homology Domain of Human Granulocyte-Colony Stimulating Factor Receptor in Escherichia coli

Ryoichi TANAKALaboratory of Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University
,
Hiroko TOKUNAGALaboratory of Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University
,
Shinichi HARAAmgen Inc., Amgen Center
,
Tsutomu ARAKAWAAmgen Inc., Amgen Center
&
Masao TOKUNAGALaboratory of Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University
Pages 1809-1811 | Received 17 Apr 1998, Published online: 22 May 2014

  • 1) Fukunaga, R., Ishizuka-Ikeda, E., Seto, Y., and Nagata, S., Expression cloning of a receptor for murine granulocyte colony-stimulating factor. Cell, 61, 341-350 (1990).
  • 2) Fukunaga, R., Seto, Y., Mizushima, S., and Nagata, S., Three different mRNAs encoding human granulocyte colony-stimulating factor receptor. Proc. Natl. Acad. Sci. U.S.A., 87, 8702-8706 (1996).
  • 3) Fukunaga, R., Ishizuka-Ikeda, E., Pan, C. X., and Seto, Y., Functional domains of the granulocyte colony-stimulating factor receptor. EMBO J., 10, 2855-2865 (1991).
  • 4) Derman, A. I., Prinz, W. A., Belin, D., and Beckwith, J., Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science, 262, 1744-1747 (1993).
  • 5) Hiraoka, O., Anaguchi, H., Yamasaki, K., Fukunaga, R., Nagata, S., and Ota, Y., Ligand binding domain of granulocyte colony-stimulating factor receptor.J. Biol. Chem., 269, 22412-22419 (1994).
  • 6) Hiraoka, O., Anabuchi, H., and Ota, Y., Formation of 1:1 complex of the cytokine receptor homologous region of granulocyte colony-stimulating factor receptor with ligand. Biosci. Biotech. Biochem., 59, 2351-2354 (1996).
  • 7) Hiraoka, O., Anaguchi, H., Asakura, A., and Ota, Y., Requirement for the immunoglobulin-like domain of granulocyte colony-stimulating factor receptor in formation of a 2:1 receptor-ligand complex. J. Biol. Chem., 270, 25928-25934 (1995).
  • 8) Haniu, M., Horan, T., Arakawa, T., Le, J., Katta, V., Hara, S., and Rohde, M. F., Disulfide structure and N-glycosylation sites of an extracellular domain of granulocyte-colony stimulating factor receptor. Biochemistry, 35, 13040-13046 (1996).
  • . 1989. p. 61- 70.
  • 10) Sanger, F., Nicklen, S., and Coulson, A. R., DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. U.S.A., 74, 5463-5467 (1977).
  • 11) Horan, T. P., Martin, F., Simonet, L., Arakawa, T., and Philo, J. S., Dimerization of granulocyte-colony stimulating factor receptor: The Ig plus CRH constract of granulocyte-colony stimulating factor receptor forms a 2:2 complex with a ligand. J. Biochem., 121, 370-375 (1997).
  • 12) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).

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