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Detection and affinity purification of β‐endorphin precursors using a monoclonal antibody
Author(s) -
Thorpe Robin,
Spitz Lidia,
Spitz Moises,
Austen Brian M.
Publication year - 1983
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(83)80353-6
Subject(s) - monoclonal antibody , sepharose , affinity chromatography , antibody , chemistry , beta (programming language) , microbiology and biotechnology , covalent bond , monoclonal , biochemistry , chromatography , enzyme , biology , immunology , computer science , organic chemistry , programming language
A monoclonal antibody to porcine β‐lipotropin has been produced which binds to the N‐terminal (λ‐lipotropin) portion of the molecule. The antibody can be used to detect β‐lipotropin as well as other β‐endorphin precursors (predominantly a M r 38000 polypeptide) using radiobinding assay or the immunoblotting technique. Purification of the peptides can be readily achieved by affinity chromatography using the monoclonal antibody covalently bound to Sepharose 4B. As the antibody recognises the N‐terminal part of β‐lipotropin, it can be used to detect and purify β‐lipotropin and other β‐endorphin precursors in the presence of β‐endorphin.