Di Pietro A, Godinot C, Bouillant M L, Gautheron D C
Biochimie. 1975;57(8):959-67. doi: 10.1016/s0300-9084(75)80218-5.
Soluble ATPase (F1) has been purified from pig heart mitochondria. The purified enzyme had a high specific activity and was homogeneous as checked by ultracentrifugation and electrofocusing. It could be dissociated into subunits by cold-treatment or sodium dodecyl sulfate denaturation. The molecular weights of the two major and three minor subunits could be estimated by sodium dodecyl sulfate gel electrophoresis. The native enzyme had an isoelectric point of 5.2 while the cold-denatured enzyme showed three main bands focusing at pH 5.0, 5.2, and 5.4. Kinetic properties (Vm and Km (atp) have been compared for the soluble and membrane bound ATPase in presence of various anions. Inhibitory effects of Quercetin and other flavonoids have been tested in order to get an insight on the interaction between ATPase and its natural inhibitor.
已从猪心线粒体中纯化出可溶性ATP酶（F1）。纯化后的酶具有较高的比活性，经超速离心和电聚焦检测呈均一性。通过冷处理或十二烷基硫酸钠变性可将其解离为亚基。两种主要亚基和三种次要亚基的分子量可通过十二烷基硫酸钠凝胶电泳进行估算。天然酶的等电点为5.2，而冷变性酶在pH 5.0、5.2和5.4处显示出三条主要条带。在各种阴离子存在的情况下，对可溶性和膜结合ATP酶的动力学性质（Vm和Km（ATP））进行了比较。为了深入了解ATP酶与其天然抑制剂之间的相互作用，测试了槲皮素和其他黄酮类化合物的抑制作用。
