采用等重碘代 TMT 标记切换法比较中间 pH 值和高 pH 值牛肉中差异 S-亚硝基化蛋白质的蛋白质组学鉴定。
Proteomics identification of differential S-nitrosylated proteins between the beef with intermediate and high ultimate pH using isobaric iodoTMT switch assay.
机构信息
Key Laboratory of Meat Processing and Quality Control, Ministry of Education China, Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
School of Food Science and Engineering, Yangzhou University, Industrial Engineering Center for Huaiyang Cuisin of Jiangsu Province, Yangzhou 225127, China.
出版信息
Meat Sci. 2021 Feb;172:108321. doi: 10.1016/j.meatsci.2020.108321. Epub 2020 Sep 25.
This study aimed to identify the differential S-nitrosylated proteins at post-mortem in beef longissimus thoracis (LT) muscles from carcasses with intermediate (5.40 < pH < 5.80, n = 6) and high (pH ≥ 6.00, n = 6) ultimate pH (pH). LT muscles were labeled with iodo-tandem mass tags (iodoTMT126-129). A total of 856 S-nitrosylated sites from 257 proteins were identified in high pH beef LT muscles. The S-nitrosylated protein intensity in high pH beef was higher compared to that of intermediate pH beef along with a large number of cysteine sites. The motif revealed that the cysteine modifications played an essential role in cellular signaling and homeostasis. In high pH beef, more up-regulated proteins were related to energy metabolism enzymes and mitochondrial dysfunction enzymes compared to down-regulated proteins which are involved in calcium homeostasis.
本研究旨在鉴定中间 pH 值（5.40 < pH < 5.80，n = 6）和高 pH 值（pH ≥ 6.00，n = 6）牛背最长肌（LT）肌肉死后差异 S-亚硝基化蛋白。用碘串联质量标签（iodoTMT126-129）标记 LT 肌肉。在高 pH 值牛肉 LT 肌肉中鉴定到 257 种蛋白质中的 856 个 S-亚硝基化位点。与中间 pH 值牛肉相比，高 pH 值牛肉的 S-亚硝基化蛋白强度更高，且半胱氨酸位点数量也更多。基序表明，半胱氨酸修饰在细胞信号和内稳态中起重要作用。与涉及钙稳态的下调蛋白相比，高 pH 值牛肉中更多上调的蛋白与能量代谢酶和线粒体功能障碍酶有关。
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