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Soluble interferon‐α receptor molecules are present in body fluids
Author(s) -
Novick D.,
Cohen B.,
Rubinstein M.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81523-o
Subject(s) - immunoprecipitation , extracellular , monoclonal antibody , microbiology and biotechnology , receptor , glycosylation , antibody , interferon , blot , chemistry , cell surface receptor , biochemistry , biology , immunology , gene
Soluble forms of the interferon‐α receptor (sIFN‐αR) were identified in human serum and urine by Western blotting with monoclonal antibodies (MAb) directed against IFN‐αR, and by immunoprecipitation (Iptn) of a covalently cross‐linked complex of IFN‐αR and [ 125 I]IFN‐α with anti IFN‐α MAb. Elevated levels or sIFN‐αR were found in sera of hairy cell leukemia patients. The soluble receptor from serum migrated as a 55 kDa protein in SDS‐PAGE, and, as expected, the cross‐linked product migrated as a 75 kDa protein. The soluble receptor from urine was found to be a protein of mol. wt. 45 kDa and its cross‐linked complex migrated as a 65 kDa protein. The calculated mol. wt. of the entire extracellular domain of the IFN‐αR prior to post‐translational modifications is 47,000. Since there are 12 potential glycosylation points in this extracellular domain, its actual mol. wt. may be its high as 70,000 Da. It is therefore concluded that sIFN‐αR molecules, corresponding to truncated forms of the extracellular domain of the cell surface IFN‐αR, are present in human serum and in normal human urine.