Ryrie I J
J Supramol Struct. 1975;3(3):242-7. doi: 10.1002/jss.400030306.
A purified preparation of the oligomycin-sensitive ATPase from yeast mitochondria has been shown to elicit an oligomycin- and uncoupler-senstitive ATP-32Pi exchange in the presence of phospholipids. Reconstitution was normally achieved by dialysis of an ATPase-phospholipid-cholate mixture. Following this procedure, vesicles with diameters between 200 and 1,500 A were seen by electron microscopy. As in mitochondria, ATPase activity in the reconstituted system was stimulated by a range of uncouplers which inhibited ATP-32Pi exchange. These and other findings suggest that the coupling mechanism may still be intact within the ATPase complex.
已证明，从酵母线粒体中纯化得到的寡霉素敏感型ATP酶制剂，在磷脂存在的情况下，会引发对寡霉素和解偶联剂敏感的ATP-32Pi交换。通常通过对ATP酶-磷脂-胆酸盐混合物进行透析来实现重组。按照此程序，通过电子显微镜观察到直径在200至1500埃之间的囊泡。与线粒体一样，重组系统中的ATP酶活性受到一系列抑制ATP-32Pi交换的解偶联剂的刺激。这些以及其他发现表明，偶联机制在ATP酶复合物中可能仍然完好无损。
