期刊
MEAT SCIENCE
卷 145, 期 -, 页码 431-439出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.meatsci.2018.07.027
关键词
Longissimus thomcis; S-nitrosylation; biotin switch assay; isobaric tags
资金
- National Natural Science Foundation of China [31571853]
The objective of this study was to identify the S-nitrosylated proteins in aging samples of pork longissimus thoracis muscle (aged 0 and 3 d) and to study the effects of exogenous S-nitrosoglutathione (GSNO, concentration at 10 and 100 mu M) treatments of aged 0 d sample. After validating modified biotin switch method, the samples were labeled with tandem mass tags (TMT126.129) for the LC-MS/MS analysis. A total of 366 peptides were identified to be S-nitrosylated corresponding to 339 proteins. Comparison of total intensity and individual S-nitrosylated sites between aging samples revealed that S-nitrosylation did occur in pork muscle during postmortem aging through possible pathways of denitrosylation and transnitrosylation. GSNO treatment groups showed a considerable number of potential cysteines could be modified with high thiol-reactivity. It was deduced that S-nitrosylation could be involved in the postmortem metabolic process possibly through the regulation of activity or function of glycolytic enzymes, calcium release, heat shock proteins, antioxidant enzymes and myofibrillar proteins.
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