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Purification and characterization of a recombinant human IgE Fcε fragment lacking the C4 domain
Author(s) -
Ikeyama Shuichi
Publication year - 1987
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(87)80474-x
Subject(s) - recombinant dna , fragment (logic) , immunoglobulin e , chemistry , domain (mathematical analysis) , characterization (materials science) , biochemistry , microbiology and biotechnology , biology , antibody , immunology , gene , materials science , computer science , nanotechnology , mathematics , algorithm , mathematical analysis
Complementary DNA of human lgE Icε fragment (residues 226–480) lacking the Cϕ domain was expressed in Escherichia coli and the product was purified by immunoaffinity chromatography on a monoclonal antibody (E12 0.02)‐Affi‐Gel 10 column. About 1.8 mg of an apparent dimer and 5.9 mg of a monomer were obtained from 65 g E. coli cells with 9.3% recovery. The purified products were found to lack more than half of the COOH‐terminal portion of the Cε3 domain. The apparent dimer showed high immunological specific activity (3.6 × 10 6 U/mg protein) comparable to that of natural human IgE when measured by commercial human IgE determination kits.