Wuytack F, Casteels R
Biochim Biophys Acta. 1980 Jan 25;595(2):257-63. doi: 10.1016/0005-2736(80)90088-7.
A (Ca2+ + Mg2+)-ATPase activity is demonstrated in the microsomal fraction of porcine coronary artery. The characteristics of the ATPase activity are compared with those of the Ca2+ transport, both measured in similar solutions. It is concluded that the (Ca2+ + Mg2+)-ATPase is related to the Ca2+ transport because: 1. Both transport and ATPase have similar low Km values for Ca2+ as well as comparable Hill coefficients. The Km values are respectively 0.34 +/- 0.03 microM [4] and 1.17 +/- 0.15 microM [6]. The Hill coefficients are n = 1.69 +/- 0.09 [4] and n = 1.23 +/- 0.17 [6]. 2. Ionophores A23187 and X537A stimulate (Ca2+ + Mg2+)-ATPase activity while they inhibit net Ca2+ accumulation by increasing the Ca2+ permeability of the membranes. 3. The V values for Ca2+ accumulation and for (Ca2+ + Mg2+)-ATPase are comparable.
在猪冠状动脉微粒体部分证实存在(Ca2+ + Mg2+)-ATP酶活性。将该ATP酶活性的特征与在相似溶液中测得的Ca2+转运的特征进行了比较。得出结论:(Ca2+ + Mg2+)-ATP酶与Ca2+转运相关,原因如下:1. 转运和ATP酶对Ca2+均具有相似的低Km值以及相当的希尔系数。Km值分别为0.34±0.03微摩尔[4]和1.17±0.15微摩尔[6]。希尔系数分别为n = 1.69±0.09[4]和n = 1.23±0.17[6]。2. 离子载体A23187和X537A刺激(Ca2+ + Mg2+)-ATP酶活性,同时它们通过增加膜对Ca2+的通透性来抑制净Ca2+积累。3. Ca2+积累和(Ca2+ + Mg2+)-ATP酶的V值相当。