Keywords

Phosphorylation, Myofibrillar Protein, ¦¬-Calpain, Degradation, Protein Kinase A, Alkaline Phosphatase

Abstract

Objective: To study the effect of phosphorylation of myofibrillar proteins on their degradation by ¦Ì-calpain. Method: Using sheep longissimus dorsi muscle myofibrillar protein as raw material, protein kinase A and alkaline phosphatase were added to catalyze the phosphorylation and dephosphorylation reactions. After the reaction, ¦Ì-calpain was added, and sodium dodecyl sulfate-polymer was added. Acrylamide gel electrophoresis (sodium dodecyl sulfate-polyacrylamide gel electrophoresis, SDS-PAGE), fluorescent staining, and Western blotting were used to determine the phosphorylation level and protein degradation degree of myofibrillar proteins. Results: The phosphorylation level of myofibrillar protein in the protein kinase A-treated group was significantly higher than that in the control group (P<0.05); the phosphorylation level of myofibrillar protein in the alkaline phosphatase-treated group was significantly lower than that in the control group (P<0.05); protein Kinase A treatment inhibits ¦Ì-calpain autolysis, reduces its activity, and prolongs its activity time; protein kinase A treatment promotes the degradation of myosin heavy chain and troponin T; alkaline phosphatase treatment promotes actin and muscle Degradation of interline proteins. Conclusion: Phosphorylation affects the degradation of myofibrillar protein by ¦Ì-calpain by acting on ¦Ì-calpain activity and myofibrillar protein.   For further details regarding this article and its research, please do not hesitate to contact our team for assistance. Original research done by Zhang Dequan, Li Xin, Li Meng, Li Zheng, Du Manting  

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