Meat Science and Muscle Biology Group, Department of Animal Science, Iowa State University, Ames, IA 50011, United States.
Meat Sci. 2014 Jan;96(1):379-84. doi: 10.1016/j.meatsci.2013.07.017. Epub 2013 Jul 19.
The objective of this study was to use proteomics to identify alterations of proteins that are related to tenderness. The longissimus dorsi (LD) were removed from ten beef carcasses at 24 h postmortem, and the two with the highest (HSP; average kg of force=6.57) and lowest star probe values (LSP; average kg of force=3.75) at 14 days postmortem were identified. Two-dimensional PAGE was used to compare the sarcoplasmic fraction of the LD from HSP and LSP steaks. A series of spots identified as phosphoglucomutase 1 (PGM1) were identified. Only the most alkaline isoform was identified as being unphosphorylated. The least phosphorylated isoform (isoform 5) had a greater density of the total protein (P<0.05) and phosphorylated protein (P<0.05) in the samples from HSP steaks compared to the samples from LSP steaks. This study illustrates the importance of identifying posttranslational modifications of proteins in the search for biomarkers.
本研究旨在利用蛋白质组学技术鉴定与嫩度相关的蛋白质变化。在宰后 24 h 从 10 个牛肉胴体中取出背最长肌(LD),并鉴定出在宰后 14 d 时具有最高(HSP;平均力值=6.57 kg)和最低探针值(LSP;平均力值=3.75 kg)的 2 块 LD。使用二维 PAGE 比较 HSP 和 LSP 牛排 LD 的肌浆部分。鉴定出一系列被鉴定为磷酸葡糖变位酶 1(PGM1)的斑点。只有最碱性的同工型被鉴定为未磷酸化。与 LSP 牛排样品相比,HSP 牛排样品中总蛋白(P<0.05)和磷酸化蛋白(P<0.05)的密度最大。本研究说明了在寻找生物标志物时,鉴定蛋白质翻译后修饰的重要性。