Quantitative phosphoproteomic analysis among muscles of different color stability using tandem mass tag labeling
Quantitative phosphoproteomic analysis among muscles of different color stability using tandem mass tag labeling
复制标题
使用串联质量标签标记对不同颜色稳定性的肌肉进行定量磷酸蛋白质组学分析
DOI:
10.1016/j.foodchem.2017.12.047
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发表时间:
2018
期刊:
影响因子:
8.8
通讯作者:
Zhang Dequan
中科院分区:
文献类型:
--
作者:
Li Zheng;Li Meng;Li Xin;Xin Jianzeng;Wang Ying;Shen Qingwu W;Zhang Dequan
A quantitative analysis of protein phosphorylation in ovine LTL muscle with different color stability was performed in the present study using TMT labeling in combination with TiO2phosphopeptide enrichment. A total of 3412 phosphopeptides assigned to 1070 phosphoproteins were identified by mass spectrometry, of which 243 proteins were detected to be differentially phosphorylated between muscles of different color stability. Among these differentially phosphorylated proteins, 27 phosphoproteins were identified to be key color-related proteins by informatics analysis. Proteins involved in carbohydrate metabolism, especially glycolytic enzymes, were the largest cluster of protein determined to be color-related. In addition, the phosphorylation of myoglobin at Ser133 plays a negative role in the regulation of meat color stability. In summary, this study revealed that the phosphorylation of some glycolytic enzymes and myoglobin at specific serine residues may play critical roles in the regulation of meat color stability.