References
- Anderson, M. J., Lonergan, S. M., & Huff-Lonergan, E. (2014). Differences in phosphorylation of phosphoglucomutase 1 in beef steaks from the longissimus dorsi with high or low star probe values. Meat Science, 96(1), 379–384. https://doi.org/https://doi.org/10.1016/j.meatsci.2013.07.017
- Baba, T., Kobayashi, H., Kawasaki, H., Mineki, R., Naito, H., & Ohmori, D. (2010). Glyceraldehyde-3-phosphate dehydrogenase interacts with phosphorylated Akt resulting from increased blood glucose in rat cardiac muscle. FEBS Letters, 584(13), 2796–2800. https://doi.org/https://doi.org/10.1016/j.febslet.2010.05.015
- Batuer, A., Patigu, A., & Jueken, A. (2012). Analysis of quality characteristics of lamb from different anatomical locations of Bashbay sheep. Xinjiang Agricultural Sciences, 49(9), 1734–1741. https://doi.org/https://doi.org/10.6048/j..1001-4330.2012.09.026
- Campagnol, P. C. B., dos Santos, B. A., Morgano, M. A., Terra, N. N., & Pollonio, M. A. R. (2011). Application of lysine, taurine, disodium inosinate and disodium guanylate in fermented cooked sausages with 50% replacement of NaCl by KCl. Meat Science, 87(3), 239–243. https://doi.org/https://doi.org/10.1016/j.meatsci.2010.10.018
- Chan, K. F., Hurst, M. O., & Graves, D. J. (1982). Phosphorylase kinase specificity. A comparative study with cAMP-dependent protein kinase on synthetic peptides and peptide analogs of glycogen synthase and phosphorylase. Journal of Biological Chemistry, 257(7), 3655–3659. https://doi.org/https://doi.org/10.1016/0165-022X(82)90005-7
- Chen, L., Li, X., Ni, N., Liu, Y., Chen, L., Wang, Z., Shen, Q. W., & Zhang, D. (2016). Phosphorylation of myofibrillar proteins in post‐mortem ovine muscle with different tenderness. Journal of the Science of Food and Agriculture, 96(5), 1474–1483. https://doi.org/https://doi.org/10.1002/jsfa.7244
- Chen, L., Li, Z., Everaert, N., Lametsch, R., & Zhang, D. (2019). Quantitative phosphoproteomic analysis of ovine muscle with different postmortem glycolytic rates. Food Chemistry, 280, 203–209. https://doi.org/https://doi.org/10.1016/j.foodchem.2018.12.056
- Cohen, P. (1982). The role of protein phosphorylation in neural and hormonal control of cellular activity. Nature, 296(5858), 613. https://doi.org/https://doi.org/10.1038/296613a0
- Conti, M. A., & Adelstein, R. S. (1981). The relationship between calmodulin binding and phosphorylation of smooth muscle myosin kinase by the catalytic subunit of 3ʹ: 5ʹcAMP-dependent protein kinase. Journal of Biological Chemistry, 256(7), 3178–3181. https://doi.org/https://doi.org/10.1088/2041-8205/792/1/L2
- Di Lisa, F., De Tullio, R., Salamino, F., Barbato, R., Melloni, E., Siliprandi, N., & Pontremoli, S. (1995). Specific degradation of troponin T and I by μ-calpain and its modulation by substrate phosphorylation. Biochemical Journal, 308(1), 57–61. https://doi.org/https://doi.org/10.1042/bj3080057
- Doumit, M. E., & Bates, R. O. (2000). Regulation of pork water holding capacity, color, and tenderness by protein phosphorylation. Pork Quality, 63(1), 17–22. https://www.researchgate.net/publication/238712632
- Ekdahl, K. N., & Ekman, P. (1985). Fructose-1, 6-bisphosphatase from rat liver. A comparison of the kinetics of the unphosphorylated enzyme and the enzyme phosphorylated by cyclic AMP-dependent protein kinase. Journal of Biological Chemistry, 260(26), 14173–14179. https://doi.org/https://doi.org/10.1016/0165-022X(85)90070-3
- Graves, J. D., & Krebs, E. G. (1999). Protein phosphorylation and signal transduction. Pharmacology & Therapeutics, 82(2–3), 111–121. https://doi.org/https://doi.org/10.1016/S0163-7258(98)00056-4
- Guo, X. Y., Peng, Z. Q., Zhang, Y. W., Liu, B., & Cui, Y. Q. (2015). The solubility and conformational characteristics of porcine myosin as affected by the presence of L-lysine and L-histidine. Food Chemistry, 170, 212–217. https://doi.org/https://doi.org/10.1016/j.foodchem.2014.08.045
- Huang, H., Larsen, M. R., & Lametsch, R. (2012). Changes in phosphorylation of myofibrillar proteins during postmortem development of porcine muscle. Food Chemistry, 134(4), 1999–2006. https://doi.org/https://doi.org/10.1016/j.foodchem.2012.03.132
- Immonen, K., & Puolanne, E. (2000). Variation of residual glycogen-glucose concentration at ultimate pH values below 5.75. Meat Science, 55(3), 279–283. https://doi.org/https://doi.org/10.1016/S0309-1740(99)00152-7
- Kwasiborski, A., Sayd, T., Chambon, C., Santé-Lhoutellier, V., Rocha, D., & Terlouw, C. (2008). Pig Longissimus lumborum proteome: Part II: Relationships between protein content and meat quality. Meat Science, 80(4), 982–996. https://doi.org/https://doi.org/10.1016/j.meatsci.2008.04.032
- Lee, Y. S., & Landry, A. B. (1992). Regulation of Ca2+ release from sarcoplasmic reticulum in skeletal muscles. Molecular and Cellular Biochemistry, 114(1–2), 105–108. https://doi.org/https://doi.org/10.1007/BF00240304
- Li, C., Zhou, G., Xu, X., Lundström, K., Karlsson, A., & Lametsch, R. (2015). Phosphoproteome analysis of sarcoplasmic and myofibrillar proteins in bovine longissimus muscle in response to postmortem electrical stimulation. Food Chemistry, 175, 197–202. https://doi.org/https://doi.org/10.1016/j.foodchem.2014.11.139
- Li, Z., Xin, L., Xing, G., Shen, Q. W., & Zhang, D. (2017). Phosphorylation prevents in vitro myofibrillar proteins degradation by μ-calpain. Food Chemistry, 218, 455–462. https://doi.org/https://doi.org/10.1016/j.foodchem.2016.09.048
- Liu, M., Wei, Y., Li, X., Quek, S. Y., Zhao, J., Zhong, H., Zhang, D., & Liu, Y. (2018). Quantitative phosphoproteomic analysis of caprine muscle with high and low meat quality. Meat Science, 141, 103–111. https://doi.org/https://doi.org/10.1016/j.meatsci.2018.01.001
- Meek, D. W., & Nimmo, H. G. (1984). Effects of phosphorylation on the kinetic properties of rat liver fructose-1, 6-bisphosphatase. Biochemical Journal, 222(1), 125–130. https://doi.org/https://doi.org/10.1042/bj2220125
- Meng, L. A., Xin, L. A., Jx, A., Zheng, L. A., Gl, A., & Yan, Z. A. (2017). Effects of protein phosphorylation on color stability of ground meat. Food Chemistry, 219, 304–310. https://doi.org/https://doi.org/10.1016/j.foodchem.2016.09.151
- Muroya, S., Ohnishi-Kameyama, M., Oe, M., Nakajima, I., Shibata, M., & Chikuni, K. (2007). Double phosphorylation of the myosin regulatory light chain during rigor mortis of bovine longissimus muscle. Journal of Agricultural and Food Chemistry, 55(10), 3998–4004. https://doi.org/https://doi.org/10.1021/jf063200o
- Perlo, F., Bonato, P., Fabre, R., Teira, G., & Tisocco, O. (2012). Combined effect of electrical stimulation, aging time and marination on quality of chicken breast fillet processed under commercial conditions. Journal of the Science of Food and Agriculture, 92(10), 2183–2187. https://doi.org/https://doi.org/10.1042/bj2220125
- Pratje, E., & Heilmeyer, L. M. G. (1972). Phosphorylation of rabbit muscle troponin and actin by a 3′, 5′‐c‐AMP‐dependent protein kinase. FEBS Letters, 27(1), 89–93. https://doi.org/https://doi.org/10.1016/0014-5793(72)80416-2
- Rardin, M. J., Wiley, S. E., Naviaux, R. K., Murphy, A. N., & Dixon, J. E. (2009). Monitoring phosphorylation of the pyruvate dehydrogenase complex. Analytical Biochemistry, 389(2), 157–164. https://doi.org/https://doi.org/10.1016/j.ab.2009.03.040
- Ravindran, S., Radke, G. A., Guest, J. R., & Roche, T. E. (1996). Lipoyl domain-based mechanism for the integrated feedback control of the pyruvate dehydrogenase complex by enhancement of pyruvate dehydrogenase kinase activity. Journal of Biological Chemistry, 271(2), 653–662. https://doi.org/https://doi.org/10.1074/jbc.271.2.653
- Sharma, R. K. (1991). Phosphorylation and characterization of bovine heart calmodulin-dependent phosphodiesterase. Biochemistry, 30(24), 5963–5968. https://doi.org/https://doi.org/10.1021/bi00238a021
- Stull, J. T., Kamm, K. E., & Vandenboom, R. (2011). Myosin light chain kinase and the role of myosin light chain phosphorylation in skeletal muscle. Archives of Biochemistry and Biophysics, 510(2), 120–128. https://doi.org/https://doi.org/10.1016/j.abb.2011.01.017
- Tahergorabi, R., Beamer, S. K., Matak, K. E., & Jaczynski, J. (2012). Salt substitution in surimi seafood and its effects on instrumental quality attributes. LWT-Food Science and Technology, 48(2), 175–181. https://doi.org/https://doi.org/10.1016/j.lwt.2012.03.004
- Wang, S., Li, C., Xu, X., & Zhou, G. (2013). Effect of fasting on energy metabolism and tenderizing enzymes in chicken breast muscle early postmortem. Meat Science, 93(4), 865–872. https://doi.org/https://doi.org/10.1016/j.meatsci.2012.11.053
- Wang, Z., Zhang, C., Li, Z., Shen, Q., & Zhang, D. (2017). Comparative analysis of muscle phosphoproteome induced by salt curing. Meat Science, 133, 19–25. https://doi.org/https://doi.org/10.1016/j.meatsci.2017.05.018
- Zeniya, M., Sohara, E., Kita, S., Iwamoto, T., Susa, K., Mori, T., Oi, K., Chiga, M., Takahashi, D., Yang, -S.-S., Lin, S.-H., Rai, T., Sasaki, S., & Uchida, S. (2013). Dietary salt intake regulates WNK3–SPAK–NKCC1 phosphorylation cascade in mouse aorta through angiotensin II. Hypertension, 62(5), 872–878. https://doi.org/https://doi.org/10.1161/HYPERTENSIONAHA.113.01543
- Zhang, C., Wang, Z., Li, Z., Shen, Q., Chen, L., Gao, L., & Zhang, D. (2016). Phosphoproteomic profiling of myofibrillar and sarcoplasmic proteins of muscle in response to salting. Food Science and Biotechnology, 25(4), 993–1001. https://doi.org/https://doi.org/10.1007/s10068-016-0161-0
- Zhang, Y., Cheng, Q., Yao, Y., Guo, X., Wang, R., & Peng, Z. (2014). A preliminary study: Saltiness and sodium content of aqueous extracts from plants and marine animal shells. European Food Research and Technology, 238(4), 565–571. https://doi.org/https://doi.org/10.1007/s00217-013-2136-1
- Zhang, Y., Guo, X., Liu, T., & Peng, Z. (2018). Effects of substitution of NaCl with KCl, L-histidine, and L-lysine on instrumental quality attributes of cured and cooked pork loin. CyTA-Journal of Food, 16(1), 877–883. https://doi.org/https://doi.org/10.1080/19476337.2018.1493538
- Zhang, Y., Wu, J., Jamali, M. A., Guo, X., & Peng, Z. (2017). Heat-induced gel properties of porcine myosin in a sodium chloride solution containing l-lysine and l-histidine. LWT-Food Science and Technology, 85, 16–21. https://doi.org/https://doi.org/10.1016/j.lwt.2017.06.059
- Zhou, C., Li, J., & Tan, S. (2014). Effect of L-lysine on the physicochemical properties of pork sausage. Food Science and Biotechnology, 23(3), 775–780. https://doi.org/https://doi.org/10.1007/s10068-014-0104-6