Boutry M, Briquet M, Goffeau A
J Biol Chem. 1983 Jul 25;258(14):8524-6.
The mitochondrial F1-ATPase from bean (Vicia faba L.) was solubilized by a chloroform treatment of mitochondrial membranes and purified by centrifugation on a glycerol gradient. The active fraction contained 5 subunits: alpha (Mr = 52,000), beta (Mr = 51,000), gamma (Mr = 34,000), delta (Mr = 23,800), and epsilon (Mr = 22,900). Purified coupled mitochondria were incubated in the presence of [ 35S ]methionine and malate to allow mitochondrial translation to occur. The largest labeled polypeptide (Mr = 52,000) was present in the chloroform extract, co-sedimented with the F1-ATPase on glycerol gradient and co-migrated with the alpha subunit upon two-dimensional electrophoresis. The results indicate that the alpha subunit of bean mitochondrial ATPase is translated on mitoribosomes, in contrast to the situation in other organisms.
通过用氯仿处理线粒体膜，可溶解蚕豆（Vicia faba L.）的线粒体F1 - ATP酶，并通过在甘油梯度上离心进行纯化。活性组分包含5个亚基：α（Mr = 52,000）、β（Mr = 51,000）、γ（Mr = 34,000）、δ（Mr = 23,800）和ε（Mr = 22,900）。将纯化的偶联线粒体在[35S]甲硫氨酸和苹果酸存在下孵育，以使线粒体翻译发生。最大的标记多肽（Mr = 52,000）存在于氯仿提取物中，在甘油梯度上与F1 - ATP酶共沉降，并且在二维电泳时与α亚基共迁移。结果表明，与其他生物的情况相反，蚕豆线粒体ATP酶的α亚基是在线粒体核糖体上翻译的。
