Nakamura J, Endo Y, Konishi K
Biochim Biophys Acta. 1977 Dec 1;471(2):260-72. doi: 10.1016/0005-2736(77)90254-1.
Membrane-bound Ca or Mg of sarcoplasmic reticulum fragments were removed by treating the membrane with EDTA or an acidic solution, and the changes in the enzymatic activities of sarcoplasmic reticulum fragments induced by these treatments were examined. With the decrease in the amount of membrane-bound Ca below 1-3-10(-8) mol/mg protein, it was demonstrated that the activity of (Ca2+ + Mg2+)-ATPase transiently increased and then diminished, that the Ca-uptake and phosphoenzyme formation declined gradually, and that the activity of Mg2+-ATPase was affected to a less extent. Sodium dodecyl sulfate-gel electrophoretic patterns of peptides from the metal-deficient membranes were the same as those of the untreated material. The level of the phosphoenzyme formation of the metal-deficient membrane was restored by increasing the amount of membrane-bound Ca, but not by increasing the amount of membrane-bound Mg.
通过用乙二胺四乙酸（EDTA）或酸性溶液处理肌浆网片段的膜，去除膜结合的钙或镁，并检测这些处理诱导的肌浆网片段酶活性的变化。随着膜结合钙量降至1 - 3×10⁻⁸摩尔/毫克蛋白质以下，结果表明（Ca²⁺ + Mg²⁺）-ATP酶活性先短暂增加然后降低，钙摄取和磷酸酶形成逐渐下降，而Mg²⁺-ATP酶活性受影响程度较小。来自缺金属膜的肽的十二烷基硫酸钠 - 凝胶电泳图谱与未处理材料的相同。通过增加膜结合钙的量可恢复缺金属膜的磷酸酶形成水平，但增加膜结合镁的量则不能。
