Abstract
Postmortem changes in proteins that have been implicated in affecting muscle integrity were examined in goose (GG) and duck (DG) gizzard smooth muscle stored at 5°C. GG and DG smooth muscles were sampled at 0, 1, 3 and 7day of storage. The pH was approximately 7 in both GG and DG samples during postmortem storage. Casein zymograms showed that 0-day μ-calpain activity was higher (p<0.05) in GG than in DG samples. As postmortem time progressed, μ-calpain was activated and autolyzed more extensively in GG than in DG samples. However, μ/m-calpain remained relatively stable in both samples. Western blots indicated that postmortem desmin degradation was more rapid in GG than in DG samples. In contrast, α-actinin remained nearly unchanged in both samples. Therefore, our results suggest that μ-calpain has an important role in the postmortem proteolysis of gizzard smooth muscle.
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