Hughes J, Joshi S, Torok K, Sanadi D R
J Bioenerg Biomembr. 1982 Dec;14(5-6):287-95. doi: 10.1007/BF00743058.
The lysolecithin extraction procedure originally described by Sadler et al. (1974) has been modified to yield a H+-ATPase with high levels of Pi-ATP exchange activity (400-600 nmol x min-1 x mg-1). This activity is further enhanced (1400-1600 nmol x min-1 x mg-1) following sucrose density gradient centrifugation in the presence of asolectin. This enhancement results in part from a lipid-dependent activation and in part from removal of inactive complexes. The H+ translocating activity of the complex has been determined spectrophotometrically using binding of oxonol VI as an indicator of membrane potential. Pi-ATP exchange, ATP hydrolysis, and oxonol binding are sensitive to energy-transfer inhibitors (oligomycin, rutamycin) and/or uncouplers (DNP, FCCP).
萨德勒等人（1974年）最初描述的溶血卵磷脂提取程序已被修改，以产生具有高水平Pi-ATP交换活性（400-600 nmol·min⁻¹·mg⁻¹）的H⁺-ATP酶。在存在大豆卵磷脂的情况下进行蔗糖密度梯度离心后，该活性进一步增强（1400-1600 nmol·min⁻¹·mg⁻¹）。这种增强部分源于脂质依赖性激活，部分源于去除无活性复合物。已使用氧杂萘酚VI的结合作为膜电位的指标，通过分光光度法测定了该复合物的H⁺转运活性。Pi-ATP交换、ATP水解和氧杂萘酚结合对能量转移抑制剂（寡霉素、鲁塔霉素）和/或解偶联剂（二硝基苯酚、羰基氰化物间氯苯腙）敏感。
