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Monoclonal antibodies to cytochrome P‐450 immunopurify a 45‐kDa protein from a human lymphoblastoid cell line
Author(s) -
Friedman Fred K.,
Pastewka Jullia V.,
Robinson Richard C.,
Park Sang Shin,
Marietta Michael A.,
Gelboin Harry V.
Publication year - 1985
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(85)80742-0
Subject(s) - monoclonal antibody , epitope , cytochrome , microbiology and biotechnology , cell culture , chemistry , antibody , lymphoblast , cytochrome c , biochemistry , biology , enzyme , immunology , mitochondrion , genetics
Monoclonal antibodies (MAbs) to rat liver cytochromes P‐450 have previously been used for successful immunopurification of cytochromes P‐450 from animal tissues. We now report application of this MAb‐based immunopurification technique to the human lymphoblastoid AHH‐1 cell line. Immunopurification carried out with 3 different MAbs each yielded a 45‐kDa polypeptide. The purified protein contains an MAb‐specific epitope present on cytochromes P‐450, and may therefore be a human cytochrome P‐450.