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Characterization of a monoclonal antibody to human sex hormone binding globulin
Author(s) -
Hammond G.L.,
Robinson P.A.
Publication year - 1984
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(84)80268-9
Subject(s) - sex hormone binding globulin , monoclonal antibody , antibody , affinity chromatography , biology , titer , globulin , microbiology and biotechnology , chemistry , biochemistry , hormone , endocrinology , androgen , immunology , enzyme
We have produced a monoclonal hybridoma cell line (S 1 B 5 ) that secretes an IgG 2α immunoglobulin with a high affinity ( K d 0.38 × 10 −11 M) for 125 I‐labelled sex hormone binding globulin (SHBG), and which will specifically immunoprecipitate SHBG from serum. The antibody is produced in high titre in culture medium and ascites fluid, and can be purified to apparent homogeneity by protein A affinity chromatography. When examined by isoelectrofocussing, a characteristic series of bands, which bind 125 I‐SHBG, are observed at pH 8.5–9. Competitive, superimposable displacement of 125 I‐SHBG from the antibody is achieved with dilutions of human, chimpanzee and gorilla sera at comparable SHBG concentrations. Partial cross‐reaction is observed with sera from other Old World primates, but not with sera from New World monkeys or any other vertebrate species studied.