Changes on the myofibrillar proteins of Sea Salmon ( Pseudopercis semifasciata ) induced by malonaldehyde were investigated. Electrophoretic patterns, solubility, and differential scanning calorimetric studies were performed after incubation of proteins with malonaldehyde (MDA) at 27 °C. Results obtained showed a different thermal behavior, evidencing a decrease in thermal stability, changes in denaturation enthalpies values (ΔH total and ΔH myosln ), and the appearance of new molecular species with a loss in the cooperativity of the myosin denaturation. A decrease in solubility and SDS‐PAGE profiles revealed the participation of myosin and other proteins in the formation of aggregates involving nondisulfide covalent linkages for myosin heavy chain (MHC) and disulfide bridges in some other proteins.
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Tironi et al. (2002) studied this question.
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