Steinman H M, Hill R L
Proc Natl Acad Sci U S A. 1973 Dec;70(12):3725-9. doi: 10.1073/pnas.70.12.3725.
Superoxide dismutase from chicken-liver mitochondria (manganese enzyme) and the two dismutases from Escherichia coli (manganese and iron enzymes) were analyzed through 29 cycles of automated Edman degradations. The high degree of homology among the amino-terminal sequences of these three dismutases corroborates their known similarity of structural and functional properties, and serves as further evidence for the endosymbiotic origin of mitochondria. In contrast, these three sequences exhibit no significant homology with the amino-terminal sequence of bovine-erythrocyte superoxide dismutase, which is consistent with the classification of eukaryotic copper-zinc dismutases as a family distinct from the manganese enzymes in stability and catalytic properties.
通过29个循环的自动埃德曼降解法分析了鸡肝线粒体超氧化物歧化酶（锰酶）和大肠杆菌的两种超氧化物歧化酶（锰酶和铁酶）。这三种超氧化物歧化酶氨基末端序列的高度同源性证实了它们已知的结构和功能特性的相似性，并进一步证明了线粒体的内共生起源。相比之下，这三个序列与牛红细胞超氧化物歧化酶的氨基末端序列没有显著同源性，这与真核铜锌超氧化物歧化酶在稳定性和催化特性方面与锰酶属于不同家族的分类一致。
