Ohta S, Harada M, Ito Y, Kobayashi Y, Sone N, Kagawa Y
Department of Biochemistry, Jichi Medical School, Tochigi, Japan.
Biochem Biophys Res Commun. 1990 Sep 28;171(3):1258-63. doi: 10.1016/0006-291x(90)90821-4.
The alpha 3 beta 3 hexamer was reconstituted from the alpha and beta subunits of TF1 portion of ATP synthase of thermophilic bacterium (Kagawa et al. (1989) FEBS Lett. 249, 67). The alpha 1 beta 1 heterodimer of ATP synthase was isolated by high performance liquid chromatography (HPLC) of the alpha 3 beta 3 hexamer in the presence of AT(D)P-Mg. On polyacrylamide gel electrophoresis, both bands corresponding to the dimer and hexamer showed ATPase activity. The alpha 1 beta 1 dimer was dissociated into the equal amounts of the alpha and beta monomers by sodium dodecyl sulfate. The alpha and beta monomers were practically inactive. The alpha 2 and beta 2 homodimers were not detected by electrophoresis and HPLC.
α3β3六聚体由嗜热菌ATP合酶TF1部分的α和β亚基重构而成（Kagawa等人，(1989)《欧洲生物化学学会联合会快报》249, 67）。在AT(D)P-Mg存在的情况下，通过对α3β3六聚体进行高效液相色谱（HPLC）分离得到ATP合酶的α1β1异二聚体。在聚丙烯酰胺凝胶电泳中，对应二聚体和六聚体的两条带均显示出ATP酶活性。α1β1二聚体被十二烷基硫酸钠解离成等量的α和β单体。α和β单体实际上没有活性。通过电泳和HPLC未检测到α2和β2同二聚体。
