Abstract

α-Actinin release and its degradation from myofibrils Z-line were studied in post mortemwhite dorsal muscle from bass and sea trout stored at 4°C and 10°C. Using α-actinin specific antibodies, we show that this protein is rapidly released within the first 24 h for the two species, and reaches a plateau within 4 days. Proteolysis take place very rapidly in bass muscle yielding 80 and 40 kDa fragments from α-actinin as major bands of proteolysis. Sea trout muscle is more resistant, and muscle stored at 4°C is not significantly α-actinin degraded even 10 days after death. In the case of sea trout muscle stored at 10°C, an increasing quantity of 80 and 40 kDa fragment can be observed after the third day. These results show that release and proteolysis of α-actinin are time- and temperature-dependent processes that take place at the early stages of fish storage. Furthermore, we observed that proteolysis of α-actinin seems to be dependent on fish species. In both species studied, the early release of α-actinin comes before the degradation of released molecules, and appears as a biphasic process throughout the disorganisation ofpost mortemmuscle in fish cold-stored above 0°C.

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