Quantitative phosphoproteomic analysis among muscles of different color stability using tandem mass tag labeling
| Autor: | Jianzeng Xin, Ying Wang, Meng Li, Qingwu W. Shen, Xin Li, Zheng Li, Dequan Zhang |
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| Rok vydání: | 2018 |
| Předmět: |
Male
Phosphopeptides Proteomics inorganic chemicals 0301 basic medicine Meat Color Tandem mass tag Analytical Chemistry Serine 03 medical and health sciences chemistry.chemical_compound Tandem Mass Spectrometry Animals Protein phosphorylation Phosphorylation Titanium Sheep Myoglobin Phosphopeptide Muscles Phosphoproteomics General Medicine Phosphoproteins 030104 developmental biology chemistry Biochemistry Glycolysis Quantitative analysis (chemistry) Food Analysis Food Science |
| Zdroj: | Food Chemistry. 249:8-15 |
| ISSN: | 0308-8146 |
| DOI: | 10.1016/j.foodchem.2017.12.047 |
| Popis: | 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 TiO2 phosphopeptide 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. |
| Databáze: | OpenAIRE |
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