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Comparative analysis of muscle phosphoproteome induced by salt curing

Wang, Zhenyu, Zhang, Caixia, Li, Zheng, Shen, Qingwu, Zhang, Dequan
Meat science 2017 v.133 pp. 19-25
actin, creatine kinase, crossbreds, databases, glycogen, glycolysis, meat quality, muscle protein, muscles, myoglobin, myosin light chains, phosphoproteins, phosphoproteome, phosphorylase, protein degradation, protein phosphorylation, salting, sheep, skeletal muscle, sodium chloride, staining, triose-phosphate isomerase, tropomyosins, troponin T, two-dimensional gel electrophoresis
Phosphorylated proteins in ovine muscle induced by salt curing were well investigated. Ten topside muscles of crossbred sheep were ground, mixed and divided into two groups, which were cured for 16h with 0% and 3% NaCl, respectively. Muscle proteins of two cured groups were analyzed by two-dimensional electrophoresis coupled with Pro-Q Diamond and SYPRO Ruby staining. The differential phosphorylated proteins were determined using LC-MS/MS and the UniProt database. Ten different phosphoproteins (>1.5 fold) induced by salting were identified, including triosephosphate isomerase, glycogen phosphorylase, creatine kinase M-type, myoglobin, troponin T fast skeletal muscle type, actin, myosin light chain 1/3, tropomyosin beta chain, etc. Most of the different phosphoproteins were involved in glycometabolism, protein function and protein degradation. It is conclusively that salting may influence meat quality through protein phosphorylation, which regulates glycolysis metabolism, protein function and degradation.