宰后肌肉中肌球蛋白磷酸化调控肌动球蛋白解离作用机制

doi:10.3864/j.issn.0578-1752.2016.16.013

Abstract

Abstract: 【Objective】The aim of this study was to investigate the effect of myosin phosphorylation modification on actomyosin dissociation by analyzing the correlation between myosin phosphorylation and actomyosin dissociation, and then reveal the function of myosin phosphorylation to sarcomere length and tenderness during postmortem.【Method】Samples of ovine longissimus dorsi after storage at 4℃ for 6, 24, 48, 72 h were collected for myosin phosphorylation and actomyosin dissociation by SDS-PAGE, Pro-Q Diamond staining and western blotting, actomyosin ATPase activity. And sarcomere length was measured by transmission electron microscope.【Result】The phosphorylation level of myosin light chain 2 decreased sharply from 0.5-48 h (P＜0.05), then it increased from 48-72 h, and the final value was lower than the initial phosphorylation value. While to the dissociation of actomyosin, it displayed a gradual decrease from 0.5-6 h and then increased from 6-48 h (P＜0.05), finally kept stable during 48-72 h postmortem, and the final dissociation degree was significantly higher than 0.5 h. The actomyosin ATPase activity increased to the highest value at 24 h, followed by gradual decrement from 24 to 72 h. On the contrary, the sarcomere length decreased to the shortest value at 24 h, followed by gradual sarcomere relaxation from 24 to 72 h.【Conclusion】The phosphorylation level of myosin light chain 2 had a great influence on myosin and actin interaction, in addition, the sarcomere contraction (myosin and actin interaction force) and the dissociation of actomyosin (myosin and actin interaction amount) happened out of sync during postmortem. Phosphorylation modification of myosin light chain 2 caused the sarcomere shrinkage and relaxation by negative regulating actomyosin dissociation and actomyosin ATPase activity negatively, which could control the final meat tenderness.

Key words: phosphorylation, myosin heavy chain, myosin light chain 2, actomyosin, dissociation, ovine longissimus dorsi

GAO Xing, LI Xin, LI Zheng, DU Man-ting, ZHANG Cai-xia, ZHANG De-quan, DING Wu. The Mechanism of Myosin Phosphorylation Regulating Actomyosin Dissociation of Skeletal Muscle During Postmortem[J].Scientia Agricultura Sinica, 2016, 49(16): 3199-3207.

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