Wang J H
J Biol Chem. 1985 Feb 10;260(3):1374-7.
A method has been developed for the effective inactivation of bovine heart mitochondrial F1-ATPase (MF1) by partially dissociating its subunits with 3 M LiCl at 0 degree C and for the subsequent partial restoration of its ATPase activity by making the subunits reassociate upon the removal of LiCl by centrifugal gel filtration at room temperature through Sephadex G-25-80 which has been pre-equilibrated with buffer containing 3 mM ATP. When covalently labeled MF1 with approximately one 7-[4-nitro-2,1,3-benzoxadiazole] label/MF1 was subjected to this type of partial dissociation-reassociation treatment, its ATPase activity could be increased from 1.48 to 18.0 mumol of ATP min-1 mg-1 without losing the covalent label. The experimental results are incompatible with models for F1-ATPase with either 3 or 2 equivalent alternating catalytic sites, but are consistent with the model with 1 active catalytic site and 2 interacting regulatory sites.
已开发出一种方法，可通过在0℃下用3M LiCl使亚基部分解离来有效灭活牛心线粒体F1 - ATP酶（MF1），随后通过在室温下通过用含3mM ATP的缓冲液预平衡的Sephadex G - 25 - 80进行离心凝胶过滤去除LiCl后使亚基重新结合，来部分恢复其ATP酶活性。当用约一个7 - [4 - 硝基 - 2,1,3 - 苯并恶二唑]标记/MF1的共价标记MF1进行这种部分解离 - 重新结合处理时，其ATP酶活性可从1.48增加到18.0 μmol ATP min⁻¹ mg⁻¹，且不会失去共价标记。实验结果与具有3个或2个等效交替催化位点的F1 - ATP酶模型不相符，但与具有1个活性催化位点和2个相互作用调节位点的模型一致。
