アクトミオシンATPアーゼ作用におよぼす二価金属イオンの効果
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概要
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We have reported that the ATPase activity modified by Mg^<++> or Ca^<++> greatly depends upon the KCl concentration (Maruyama and Ishikawa, 1963). The Mg-enhanced ATPase activity is high at low KCl concentrations (<0.03M) with superprecipitation, and low at moderate KCl concentrations (>0.08M) with clearing response (cf. Maruyama and Gergely, 1962a, b). On the other hand, the Ca-activated ATPase activity increases as the KCl concentration is raised to 0.15M. In the present study the effects of various divalent metals were compared with those of Mg^<++> and Ca^<++>. Experimental techniques are referred to in a previous article (Maruyama and Ishikawa, 1964). As can be clearly seen in figs. 1 and 2, of the metals tested, only Mn^<++> behaved similarly to Mg^<++>, although the KCl concentrations at which Mn^<++> induced clearing were found to be higher than those at which Mg^<++> induced clearing. Maruyama and Gergely (1962b) were unable to demonstrate the clearing effect of Mn^<++> at 0.15M KCl, probably because a rather high concentration of reconstituted actomyosin was used, which was more superprecipitable than natural actomyosin. The effects of Co^<++>, Sn^<++>, Sr^<++>, and Ba^<++> were similar to that of Ca^<++>, except that activation was less than with Ca^<++>. The effects of Ni^<++> and Fe^<++> were independent of KCl concentration. Cd^<++> and Zn^<++>, in a concentration of 1mM, abolished the ATPase activity. This work was supported by a grant-in-aid from the Muscular Dystrophy Associations of America, Inc.
- 社団法人日本動物学会の論文
- 1964-07-15
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