イカ肉ミオシン区蛋白の特異性について-I : ミオシン区蛋白の沈澱性状の時間的変化

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It was found in preliminary experiments that “myosins” of squid muscle are apt to become soluble at lower ionic strengths (I) and often escape from estimation (Table 1). The present work was planned to comfirm this and to find factors involved in this change. The muscles of different freshness were extracted with KCl-phosphate buffer of I=0.6 and pH ?? 7.5, myosins in the extract being determined by dilution method in three ways, immediately after the extraction, after keeping it at 30°C. for 2 hr., and after 2 day cold storage. In every case, myosins were precipitated at pH 6.5, 7 and also 9 (Fig. 1). Myosins of squid was found to become less precipitable, unless the extract was diluted immediately after extraction. This change was more marked in media of pH higher than 7, and when the used muscle was not fresh (Figs. 3 and 4). Consequently in determination of myosins in squid muscle, myosins should be precipitated immediately after extraction and at pH near and not excceeding 7. Observation of streaming birefringence of the extract suggested that asymmetry of dissolved proteins might hardly change even under the above condition which causes decrease of precipitability of myosins in the extract. With carp muscle, on the other hand, no such marked change in amount of precipitating myosins was observed (Figs. 6 and 7). ?? A protein fraction which precipitates at lower ionic strenghts (I=0.05-0.2) from saltextracts was called here “myosins”.
公益社団法人日本水産学会の論文

イカ肉ミオシン区蛋白の特異性について-I : ミオシン区蛋白の沈澱性状の時間的変化

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