Short exposure of albumin to high concentrations of malondialdehyde does not mimic physiological conditions |
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Authors: | Susanna Millanta Anna Lisa Furfaro Paolo Carlier Bruno Tasso Mariapaola Nitti Cinzia Domenicotti Patrizio Odetti Maria Adelaide Pronzato Nicola Traverso |
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Affiliation: | 1. Department of Experimental Medicine, Section of General Pathology, University of Genova, Italy;2. Immunohematology Service, University Hospital San Martino, Genova, Italy;3. DISCIFAR, University of Genova, Italy;4. Department of Internal Medicine, University of Genova, Italy |
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Abstract: | Malondialdehyde (MDA), a major lipid peroxidation product, spontaneously binds to, and modifies proteins. In vivo, proteins are physiologically exposed to micromolar MDA concentrations for long periods. In order to mimic this process in vitro, protein modification is often performed by short exposure to millimolar MDA concentrations, also in order to generate antigenic structures for antibody production. |
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Keywords: | BSA, Bovine serum albumin HNE, 4-hydroxynonenal MDA, Malondialdehyde |
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