{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,13]],"date-time":"2026-05-13T02:30:07Z","timestamp":1778639407090,"version":"3.51.4"},"reference-count":34,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2019,11,14]],"date-time":"2019-11-14T00:00:00Z","timestamp":1573689600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100010038","name":"Earmarked Fund for China Agriculture Research System","doi-asserted-by":"publisher","award":["CARS\u201038"],"award-info":[{"award-number":["CARS\u201038"]}],"id":[{"id":"10.13039\/501100010038","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31771995"],"award-info":[{"award-number":["31771995"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["scijournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["J Sci Food Agric"],"published-print":{"date-parts":[[2020,1,30]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:title>BACKGROUND<\/jats:title><jats:p>Phosphorylation is one of the most important post\u2010translational modifications. Currently, many postmortem protein phosphorylation studies in muscle have been related to meat quality such as tenderness and color stability. However, the effects of various storage temperatures (25, 15, 4 and\u2009\u22121.5\u2009\u00b0C) on the phosphorylation level of protein are poorly understood. Changes in the protein phosphorylation levels in postmortem ovine muscle at various storage temperatures were determined in this study.<\/jats:p><\/jats:sec><jats:sec><jats:title>RESULTS<\/jats:title><jats:p>The obtained data showed that pH decline rate was significantly inhibited at \u22121.5\u2009\u00b0C from 12\u2009h to 7\u2009days postmortem (<jats:italic>P<\/jats:italic>\u2009&lt;\u20090.05). The ATP consumption rate was higher at 25\u2009\u00b0C than that at other three temperatures (<jats:italic>P<\/jats:italic>\u2009&lt;\u20090.05). Analysis of the temperature, pH and ATP content revealed that the ATP content was related to the phosphorylation levels of individual protein bands. Phosphorylated myofibrillar and sarcoplasmic proteins, such as myosin binding protein C, troponin T3, myosin light chain 1, glucose\u20106\u2010phosphate isomerase and pyruvate kinase, were mainly involved in glycolysis and muscle contraction.<\/jats:p><\/jats:sec><jats:sec><jats:title>CONCLUSION<\/jats:title><jats:p>The global and specific protein phosphorylation levels can be influenced by the postmortem storage temperature of muscle. Phosphorylation of proteins was correlated with glycolysis and muscle contraction. Certain phosphorylated proteins, such as heat shock proteins, require further study to clarify their effects on meat traits. \u00a9 2019 Society of Chemical Industry<\/jats:p><\/jats:sec>","DOI":"10.1002\/jsfa.10045","type":"journal-article","created":{"date-parts":[[2019,10,6]],"date-time":"2019-10-06T04:32:54Z","timestamp":1570336374000},"page":"551-559","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":27,"title":["Effects of temperature on protein phosphorylation in postmortem muscle"],"prefix":"10.1002","volume":"100","author":[{"given":"Chi","family":"Ren","sequence":"first","affiliation":[{"name":"Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro\u2010Product Processing, Ministry of Agriculture and Rural Affairs  Beijing 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