【摘要】 从基因突变的F1 ATP酶 (基因突变质粒 ,α C193S ,γ S10 7C ,β亚基带有 10个组氨酸标记 (His Tag) ,转入到菌株大肠杆菌JM10 3)的菌株中筛选出一高表达菌株 .该菌株表达的F1 ATP酶经纯化后其水解活性明显高于文献值 .从单分子水平上进行观察 ,发现在水解ATP过程中 ,γ亚基上连接的荧光标记蛋白微丝 ,其旋转速度要比文献中同样条件下快约一倍更多还原

【Abstract】 The high activity F 1 ATPase (the mutant α C193S, γ S107C, a ten histidine (His) tag inserted immediately downstream of the β initiation codon, α 3β 3γ subcomplex) of thermophilic Bacillus PS3 was purified from E.coli . JM103 Δ( uncB uncD ),in which the majority of F 1 ATPase genes have been eliminated. It was found that the enzyme hydrolyzed ATP more efficiently than previous papers. During the F 1 ATPase hydrolyzing ATP, the rotary rate of the fluorescent actin filament attached to γ subunit of F 1 ATPase was about one times faster than that of previous papers in the similar conditions.更多还原