Deckers-Hebestreit G, Steffens K, Altendorf K
J Biol Chem. 1986 Nov 15;261(32):14878-81.
Subunit c of the membrane-integrated, proton-translocating F0 portion of the ATP synthase (F1F0) from Escherichia coli has been isolated under nondenaturing conditions (Schneider, E., and Altendorf, K. (1985) EMBO J. 4, 515-518) and antibodies have been raised in rabbits. The primary antisera did not recognize the antigen when present in the same buffer as used for the immunization. Surprisingly, in one of the three antisera a strong antibody binding was observed when intact F0, a.c complex or reconstituted subunit c was provided as the antigen. Incorporation of subunit c into liposomes together with subunits a and b forming an active, H+-translocating complex was not required for the recognition by the antiserum. Subunit c prepared by chloroform/methanol extraction or by chromatography in the presence of sodium dodecyl sulfate was not recognized by the anti-c antiserum when incorporated into liposomes.
已在非变性条件下分离出大肠杆菌ATP合酶（F1F0）的膜整合质子转运F0部分的亚基c（施奈德，E.，和阿尔滕多夫，K.（1985年）《欧洲分子生物学组织杂志》4，515 - 518），并在兔体内产生了抗体。当存在于与免疫所用相同的缓冲液中时，初级抗血清无法识别抗原。令人惊讶的是，在三种抗血清中的一种中，当提供完整的F0、a.c复合物或重组亚基c作为抗原时，观察到了强烈的抗体结合。抗血清识别并不需要将亚基c与亚基a和b一起掺入脂质体中形成活性H +转运复合物。通过氯仿/甲醇提取或在十二烷基硫酸钠存在下进行色谱法制备的亚基c，当掺入脂质体时不被抗c抗血清识别。
