Heron C, Smith S, Ragan C I
Biochem J. 1979 Aug 1;181(2):435-43. doi: 10.1042/bj1810435.
Purified preparations of Complex I (NADH-ubiquinone oxidoreductase) from bovine heart mitochondria may be resolved into 26 polypeptides by two-dimensional analysis combining isoelectric focusing and polyacrylamide-gel electrophoresis in sodium dodecyl sulphate. Similar analyses of the fragments obtained from chaotropic resolution of the enzyme show that each of these fragments contains a distinct and non-overlapping set of polypeptides. Evidence that the polypeptides seen in the intact enzyme are true constituents comes from analyses of immunoprecipitates obtained by allowing Complex I or solubilized submitochondrial particles to react with antisera directed against the whole enzyme and a subfragment of the enzyme.
通过等电聚焦和十二烷基硫酸钠聚丙烯酰胺凝胶电泳相结合的二维分析，牛心线粒体中纯化的复合体I（NADH - 泛醌氧化还原酶）制剂可分解为26种多肽。对该酶经离液剂分解得到的片段进行的类似分析表明，这些片段中的每一个都含有一组不同且不重叠的多肽。完整酶中所见多肽是真实组成成分的证据来自于对免疫沉淀物的分析，这些免疫沉淀物是通过使复合体I或溶解的亚线粒体颗粒与针对全酶及其一个亚片段的抗血清反应而获得的。
