Kauffer S, Schmid R, Steffens K, Deckers-Hebestreit G, Altendorf K
Arbeitsgruppe Mikrobiologie, Universität Osnabrück, Federal Republic of Germany.
Arch Microbiol. 1987 Sep;148(3):187-92. doi: 10.1007/BF00414810.
The ATP synthase complex of Klebsiella pneumoniae (KF1F0) has been purified and characterized. SDS-gel electrophoresis of the purified F1F0 complexes revealed an identical subunit pattern for E. coli (EF1F0) and K. pneumoniae. Antibodies raised against EF1 complex and purified EF0 subunits recognized the corresponding polypeptides of EF1F0 and KF1F0 in immunoblot analysis. Protease digestion of the individual subunits generated an identical cleavage pattern for subunits alpha, beta, gamma, epsilon, a, and c of both enzymes. Only for subunit delta different cleavage products were obtained. The isolated subunit c of both organisms showed only a slight deviation in the amino acid composition. These data suggest that extensive homologies exist in primary and secondary structure of both ATP synthase complexes reflecting a close phylogenetic relationship between the two enterobacteric tribes.
肺炎克雷伯菌的ATP合酶复合体（KF1F0）已被纯化并进行了特性分析。纯化后的F1F0复合体的SDS凝胶电泳显示，大肠杆菌（EF1F0）和肺炎克雷伯菌具有相同的亚基模式。在免疫印迹分析中，针对EF1复合体产生的抗体和纯化的EF0亚基识别出了EF1F0和KF1F0的相应多肽。对单个亚基进行蛋白酶消化后，两种酶的α、β、γ、ε、a和c亚基产生了相同的切割模式。只有δ亚基获得了不同的切割产物。两种生物体分离出的c亚基在氨基酸组成上仅表现出轻微差异。这些数据表明，两种ATP合酶复合体在一级和二级结构上存在广泛的同源性，这反映了两个肠杆菌族之间密切的系统发育关系。
