Friedl P, Friedl C, Schairer H U
Eur J Biochem. 1979 Oct;100(1):175-80. doi: 10.1111/j.1432-1033.1979.tb02046.x.
The ATP synthetase of Escherichia coli K12 was purified by a simple procedure. The dicyclohexylcarbodiimide-sensitive ATPase activity was enriched 21-fold. The ATP synthetase preparation contained the eight polypeptides (alpha, beta, gamma, a,delta, b,espilon, c) of the enzyme and a residual contamination (4% of the total protein) as shown by dodecylsulfate/polyacrylamide electrophoresis. The polypeptide c was specifically labelled with [14C]dicyclohexylcarbodiimide. Energy-transducing activities were reconstituted from soybean phospholipids and the purified enzyme. The proteoliposomes exhibited a significantly higher ATP-32Pi exchange activity and a higher proton-translocating activity as compared to the untreated membranes.
通过一个简单的程序纯化了大肠杆菌K12的ATP合酶。对二环己基碳二亚胺敏感的ATP酶活性提高了21倍。如十二烷基硫酸盐/聚丙烯酰胺电泳所示，ATP合酶制剂包含该酶的8种多肽（α、β、γ、a、δ、b、ε、c）以及残留污染物（占总蛋白的4%）。多肽c被[14C]二环己基碳二亚胺特异性标记。从大豆磷脂和纯化的酶中重建了能量转换活性。与未处理的膜相比，蛋白脂质体表现出显著更高的ATP-32Pi交换活性和更高的质子转运活性。
