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

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 7 day 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.

• Authors: Ya-Shiou Chang, Marvin H Stromer, Rong-Ghi R Chou
• Journal: Food chemistry (Food Chem) Vol. 139 Issue 1-4 Pg. 384-8 (Aug 15 2013) ISSN: 1873-7072 [Electronic] England
• PMID: 23561121 (Publication Type: Journal Article)
• Copyright: Copyright © 2013 Elsevier Ltd. All rights reserved.

Chemical References

• Avian Proteins
• Desmin
• Actinin
• Calpain
• mu-calpain

Topics

• Actinin (metabolism)
• Animals
• Avian Proteins (metabolism)
• Calpain (metabolism)
• Desmin (metabolism)
• Ducks (metabolism)
• Geese (metabolism)
• Gizzard, Avian (metabolism)
• Hydrogen-Ion Concentration
• Muscle, Smooth (chemistry, enzymology)
• Postmortem Changes
• Proteolysis