Daily O P, Cuttitta F F, MacQuillan A M
Biochim Biophys Acta. 1976 Dec 1;454(2):375-81. doi: 10.1016/0005-2787(76)90239-2.
Mitochondria isolated from haploid yeast cells by spheroplast lysis were purified by flotation on renografin gradients. Electron micrographs and respiratory control ratios revealed that the purified mitochondria were still intact and functional. Assays for photoreactivation enzyme using as substrate [3H]-thymine-labeled Escherichia coli DNA were performed on crude and purified mitochondrial preparations. While the crude preparation contained high amounts of photoreactivation enzyme, it appeared to be associated with contaminating nuclei. The purified mitochondria lacked any photoreactivation enzyme activity. We suggest that yeast mitochondria do not normally contain photoreactivation enzyme.
通过原生质球裂解从单倍体酵母细胞中分离出的线粒体,在泛影葡胺梯度上浮法中进行纯化。电子显微镜照片和呼吸控制率显示,纯化后的线粒体仍然完整且具有功能。使用[3H] - 胸腺嘧啶标记的大肠杆菌DNA作为底物,对粗制和纯化的线粒体制剂进行光复活酶测定。虽然粗制制剂含有大量的光复活酶,但它似乎与污染的细胞核有关。纯化后的线粒体缺乏任何光复活酶活性。我们认为酵母线粒体通常不含有光复活酶。