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Amino acid sequence analysis of a mouse interleukin 5 receptor protein reveals homology with a mouse interleukin 3 receptor protein

(1991) EUROPEAN JOURNAL OF IMMUNOLOGY. 21(5). p.1315-1317
Author
Organization
Abstract
A polypeptide chain for the mouse interleukin 5 receptor (IL5R) was purified from detergent-lysed B13 cells, a mouse IL5-dependent pre-B cell line. Purification was by a single immunoaffinity chromatographic step using an anti-mouse IL5R monoclonal antibody, R52. Internal amino acid sequence was obtained from four trypsin-generated peptides. All peptides were found to be present in the published amino acid sequence of a mouse IL3R and the mouse IL3R-like protein deduced from the cDNA. This indicates that the mouse IL5R and the mouse IL3R have a homologous polypeptide in common and suggests that the specificity of these lymphokine receptors is mainly generated by association with another ligand-specific polypeptide chain.
Keywords
CELLS, MEMBER, CLONING, IDENTIFICATION, GENE FAMILY, EXPRESSION, IL-5

Citation

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Chicago
Devos, René, Joël Vandekerckhove, Antonius Rolink, Geert Plaetinck, José Van der Heyden, Walter Fiers, and Jan Tavernier. 1991. “Amino Acid Sequence Analysis of a Mouse Interleukin 5 Receptor Protein Reveals Homology with a Mouse Interleukin 3 Receptor Protein.” European Journal of Immunology 21 (5): 1315–1317.
APA
Devos, René, Vandekerckhove, J., Rolink, A., Plaetinck, G., Van der Heyden, J., Fiers, W., & Tavernier, J. (1991). Amino acid sequence analysis of a mouse interleukin 5 receptor protein reveals homology with a mouse interleukin 3 receptor protein. EUROPEAN JOURNAL OF IMMUNOLOGY, 21(5), 1315–1317.
Vancouver
1.
Devos R, Vandekerckhove J, Rolink A, Plaetinck G, Van der Heyden J, Fiers W, et al. Amino acid sequence analysis of a mouse interleukin 5 receptor protein reveals homology with a mouse interleukin 3 receptor protein. EUROPEAN JOURNAL OF IMMUNOLOGY. 1991;21(5):1315–7.
MLA
Devos, René, Joël Vandekerckhove, Antonius Rolink, et al. “Amino Acid Sequence Analysis of a Mouse Interleukin 5 Receptor Protein Reveals Homology with a Mouse Interleukin 3 Receptor Protein.” EUROPEAN JOURNAL OF IMMUNOLOGY 21.5 (1991): 1315–1317. Print.
@article{1925360,
  abstract     = {A polypeptide chain for the mouse interleukin 5 receptor (IL5R) was purified from detergent-lysed B13 cells, a mouse IL5-dependent pre-B cell line. Purification was by a single immunoaffinity chromatographic step using an anti-mouse IL5R monoclonal antibody, R52. Internal amino acid sequence was obtained from four trypsin-generated peptides. All peptides were found to be present in the published amino acid sequence of a mouse IL3R and the mouse IL3R-like protein deduced from the cDNA. This indicates that the mouse IL5R and the mouse IL3R have a homologous polypeptide in common and suggests that the specificity of these lymphokine receptors is mainly generated by association with another ligand-specific polypeptide chain.},
  author       = {Devos, Ren{\'e} and Vandekerckhove, Jo{\"e}l and Rolink, Antonius and Plaetinck, Geert and Van der Heyden, Jos{\'e} and Fiers, Walter and Tavernier, Jan},
  issn         = {0014-2980},
  journal      = {EUROPEAN JOURNAL OF IMMUNOLOGY},
  keyword      = {CELLS,MEMBER,CLONING,IDENTIFICATION,GENE FAMILY,EXPRESSION,IL-5},
  language     = {eng},
  number       = {5},
  pages        = {1315--1317},
  title        = {Amino acid sequence analysis of a mouse interleukin 5 receptor protein reveals homology with a mouse interleukin 3 receptor protein},
  url          = {http://dx.doi.org/10.1002/eji.1830210533},
  volume       = {21},
  year         = {1991},
}

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