Key result
Fish myosin exhibits species-specific structural stability that is deeply dependent on environmental habitat temperature and is influenced by F-actin binding, light chains, and filament formation.
This review summarizes the structural stability and denaturation mechanisms of species-specific fish myosin.
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May inform species-specific fish processing; leaves open mechanistic validation of temperature and binding factors.
This presentation is a review of the development in the fish muscle protein research, especially myosin. Species-specificity of fish myosin was classified into the following four categories. 1) Structural stability of fish myosin as studied by the denaturation caused by heating, freezing, urea etc. Thermal stability of fish myosin deeply dependent on the environmental temperature is discussed. 2) Structural stability of myosin filaments as investigated by the actin-activated Mg-ATPase activity. 3) Myosin stabilization upon F-actin binding in connection with the accelerated denaturation by salt and pyrophosphate (PPi). Myosin denaturation mode in myofibrils was also discussed. 4) Light chain (LC) binding and its effect on myosin denaturation.
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KUNTHIKO KONNO (2002) reported a review. Fish myosin structural stability was evaluated. Fish myosin exhibits species-specific structural stability that is deeply dependent on environmental habitat temperature and is influenced by F-actin binding, light chains, and filament formation.
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