mu-Calpain is involved in the postmortem proteolysis of gizzard smooth muscle

作者：Chang Ya Shiou; Stromer Marvin H; Chou Rong Ghi R^*

来源：Food Chemistry, 2013, 139(1-4): 384-388.

DOI：10.1016/j.foodchem.2013.01.075

• Gizzard smooth muscle
• Postmortem proteolysis
• Calpain
• Desmin

Postmortem changes in proteins that have been implicated in affecting muscle integrity were examined in goose (CC) and duck (DG) gizzard smooth muscle stored at 5 degrees C. GG and DG smooth muscles were sampled at 0, 1,3 and 7 day of storage. The pH was approximately 7 in both GG and DG samples during postmortem storage. Casein zymograms showed that 0-day mu-calpain activity was higher (p %26lt; 0.05) in GG than in DG samples. As postmortem time progressed, mu-calpain was activated and autolyzed more extensively in GG than in DC samples. However, mu/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, alpha-actinin remained nearly unchanged in both samples. Therefore, our results suggest that mu-calpain has an important role in the postmortem proteolysis of gizzard smooth muscle.

• 出版日期2013-7-1