Immunoassays for proteins alkylated by nicotine-derived N-nitrosamines |
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Authors: | Brian Talbot Serge Desnoyers Andre Castonguay |
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Affiliation: | (1) Department of Biology, Faculty of Sciences, University of Sherbrooke, J1K 2R1 Sherbrooke, Québec, Canada;(2) Laboratory of Cancer Etiology and Chemoprevention, School of Pharmacy, Laval University, G1K 7P4 Quebec Q. C, Canada |
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Abstract: | Polyclonal antibodies recognizing the pyridyloxobutyl (POB) moiety of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) were produced in rabbits immunized either with POB-bovine albumin or POB-Sepharose. The POB intermediates necessary to modify the protein were generated by alkaline (pH 9.0) treatment of the synthetic precursor 4-(carbethoxynitrosamino)-1-(3-pyridyl)-1-butanone. In a competitive enzyme linked immunoabsorbent assay (ELISA), 70 pmole NNK inhibited 50% of the binding of the anti-POB antibodies to POB-protein absorbed on microtiterplates. This 50% inhibition varied from 70 pmole to 200 nmole using a series of NNK analogues, depending on the integrity of the POB moiety. Immunological techniques initiated in this study detect NNK-protein conjugates or measure the quantity of POB groups liberated upon alkaline or acid treatment of NNK modified protein. |
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Keywords: | Carcinogen-protein adducts Tobacco-specific N-nitrosamines Dosimeter of carcinogen exposure Immunoassay |
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