采用超声波破碎茵体、DEAE阴离子柱和Superdex200分子筛柱联用法得到较纯的F0F1-ATPase全酶,并得到SDS-PAGE电泳和动态光散射检测确认。动态光散射检测显示,FOF1-ATPase分子团尺寸随温度升高而增加,不同于普通胶体和单亚基蛋白,判断与FOF1-ATPase的多亚基结构有关。研究表明,动态光散射技术是检测蛋白质均一性和稳定性的有效手段。 The pure F0F1-ATPase holoenzyme was obtained by using ultrasonic disintegration, DEAE anion column and Superdex200 molecular sieve column, and confirmed by SDS-PAGE electrophoresis and dynamic light scattering. Dynamic light scattering detection showed that FOF1-ATPase molecular size increased with increasing temperature, which was different from common colloidal and mono-subunit proteins and was related to the structure of FOF1-ATPase. Studies have shown that dynamic light scattering is an effective means of detecting protein homogeneity and stability.