Hincke M T, Demaille J G
Biochim Biophys Acta. 1984 Apr 11;771(2):188-94. doi: 10.1016/0005-2736(84)90532-7.
Calmodulin has been shown to activate the ATP-dependent Ca2+ uptake in inside-out vesicles which have been prepared from rabbit synaptosomal plasma membranes by the methodology of Gill et al. (Gill, D.L., Grollman, E.F. and Kohn, L.D. (1981) J. Biol. Chem. 256, 184-192). Following extensive washings of these membranes with EGTA/EDTA solutions, the Ca2+ uptake activity demonstrated an affinity for calmodulin of 30 nM and an affinity for Ca2+ of 2 microM. The activity was completely inhibited by the anticalmodulin compound R24571 (Ki congruent to 8 microM). The molecular weight of the ATPase molecule, revealed by a combination of the [125I]calmodulin overlay technique and [32P]phosphoenzyme electrophoresis, was 145 000. The overlay technique also revealed that the mechanism of activation is via a direct binding of calmodulin to the pump molecule.
钙调蛋白已被证明能激活通过吉尔等人（吉尔，D.L.，格罗曼，E.F.和科恩，L.D.（1981年）《生物化学杂志》256，184 - 192）的方法从兔突触体细胞膜制备的内翻小泡中依赖ATP的Ca2+摄取。用EGTA/EDTA溶液对这些膜进行大量洗涤后，Ca2+摄取活性显示对钙调蛋白的亲和力为30 nM，对Ca2+的亲和力为2 microM。该活性被抗钙调蛋白化合物R24571（Ki约为8 microM）完全抑制。通过[125I]钙调蛋白覆盖技术和[32P]磷酸化酶电泳相结合揭示的ATP酶分子的分子量为145000。覆盖技术还表明激活机制是通过钙调蛋白与泵分子的直接结合。
