魚類筋肉構成たんぱく質に関する研究-6,7-コイ筋肉ミオシン,アクトミオシンの希釈沈殿法による精製

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It has been believed that the tendency of fish myosin to denature is much greater than that of rabbit during repeated precipitation by dilution. An investigation was made to purify carp myosin and actomyosin by the usual dilution method. The preparations obtained at each step of precipitation were characterized by measuring ATP-ase activity, ATP-sensitivity, and activities of other contaminating enzymes (myokinase and adenylic deaminase). Crude myosin usually had ATP-sensitivity of 5-20. Some which had slightly higher values were improved by an intermediate precipitation at a KCl concentration of 0.28 mole/l. The crude preparations of myosin and actomyosin usually contained myokinase and adenylic deaminase. The repeated precipitation resulted in virtually complete removal of myokinase but not of adenylic deaminase. It was observed that specific ATP-ase activity of myosin preparations decreased slightly during repeated precipitation by dilution, while those of actomyosin preparations remained almost constant. The above results suggest that myosin denaturates slightly during repeated precipitation by dilution.
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