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Short exposure of albumin to high concentrations of malondialdehyde does not mimic physiological conditions
Authors:Susanna Millanta  Anna Lisa Furfaro  Paolo Carlier  Bruno Tasso  Mariapaola Nitti  Cinzia Domenicotti  Patrizio Odetti  Maria Adelaide Pronzato  Nicola Traverso
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
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.
Keywords:BSA, Bovine serum albumin   HNE, 4-hydroxynonenal   MDA, Malondialdehyde
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