Kopecký J, Houstĕk J, Drahota Z
Mol Cell Biochem. 1977 Dec 29;18(2-3):77-80. doi: 10.1007/BF00280271.
Soluble, oligomycin-insensitive ATPase released from beef heart mitchondria by chloroform extraction can be further purified by Sepharose 6B gel filtration. This purification increases enzyme activity 4--5 times (100-130U/mg). According to specific activity, high purity and ability to reconstitute oligomycin-sensitive complex, isolated ATPase is quite comparable with enzyme preparations isolated by other methods.
通过氯仿抽提从牛心线粒体中释放出的可溶性、对寡霉素不敏感的ATP酶,可经琼脂糖6B凝胶过滤进一步纯化。这种纯化使酶活性提高了4至5倍(100 - 130U/mg)。根据比活性、高纯度以及重组寡霉素敏感复合物的能力,分离得到的ATP酶与通过其他方法分离得到的酶制剂相当。