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
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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
Zhang Dequan
中科院分区:
农林科学1区
文献类型:
--
作者:
Li Zheng;Li Meng;Li Xin;Xin Jianzeng;Wang Ying;Shen Qingwu W;Zhang Dequan

文献摘要

被引文献

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本研究使用 TMT 标记结合 TiO2 磷酸肽富集,对具有不同颜色稳定性的绵羊 LTL 肌肉中的蛋白质磷酸化进行定量分析。通过质谱法鉴定出总共 3412 个磷酸肽,分配给 1070 个磷蛋白,其中 243 个蛋白质被检测到在不同颜色稳定性的肌肉之间存在差异磷酸化。在这些差异磷酸化的蛋白质中,通过信息学分析鉴定出27种磷酸化蛋白质是关键的颜色相关蛋白质。参与碳水化合物代谢的蛋白质,尤其是糖酵解酶,是确定与颜色相关的最大蛋白质簇。此外,肌红蛋白Ser133位点的磷酸化对肉色稳定性的调节起着负面作用。总之,这项研究表明,一些糖酵解酶和肌红蛋白在特定丝氨酸残基上的磷酸化可能在肉色稳定性的调节中发挥关键作用。
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.