کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
7585873 | 1492043 | 2018 | 39 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Quantitative phosphoproteomic analysis among muscles of different color stability using tandem mass tag labeling
ترجمه فارسی عنوان
تجزیه و تحلیل کمی فسفوپروتومی در عضلات پایداری رنگ های مختلف با استفاده از برچسب زدن تاندوم
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کلمات کلیدی
رنگ گوشت، فسفر پروتئومیکس، متابولیسم کربوهیدرات، آنزیم گلیکولیتیک، میوگلوبین،
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 249, 30 May 2018, Pages 8-15
Journal: Food Chemistry - Volume 249, 30 May 2018, Pages 8-15
نویسندگان
Zheng Li, Meng Li, Xin Li, Jianzeng Xin, Ying Wang, Qingwu W. Shen, Dequan Zhang,