カルシウム活性のアクトミオシンATPアーゼ作用におよぼす塩化カリ濃度と温度の影響

概要

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We have reported that the Ca-enhanced ATPase activity of actomyosin was quite low at low KCl concentrations, e. g., 0.01M, and it was greatly elevated as the KCl concentration increased up to about 0.1M (Maruyama and Ishikawa, 1963). In the present study this was verified at temperatures higher than about 15℃, but it was shown that at low temperatures of 0° to 5℃ the optimal KCl concentration for the Ca-enhanced ATPase activity was between 0.06 and 0.08M (Fig. 1). Furthermore, the activity at 0.01M KCl was roughly equal to that at 0.1M KCl at these low temperatures. The effect of varied temperature on the Caactivated ATPase action at various KCl concentrations is presented in Fig. 2. It should be mentioned that Arrhenius plots of the ATPase activity did not give a straight line except for the case at 0.01M KCl, Where the apparent activation energy was as small as 4.5 kcal. At other KCl concentrations, a break in the plot was observed at 10℃. The apparent activation energy was about 8 kcal between 10 and 30℃ and 15 kcal between 0 and 10℃, respectively, for various KCl concentrations. This work was supported by a grant from the Muscular Dystrophy Associations of America, Inc.
社団法人日本動物学会の論文
1964-04-15