鸟类和鱼类心脏线粒体细胞色素c氧化酶的分离与特性分析
Isolation and characterization of cytochrome c oxidase from bird and fish heart mitochondria.
作者信息
Montecucco C, Schiavo G, Bacci B, Bisson R
机构信息
Centro C.N.R. Fisiologia Mitocondri, Università di Padova, Italy.
出版信息
Comp Biochem Physiol B. 1987;87(4):851-6. doi: 10.1016/0305-0491(87)90401-9.
PMID:2822348
Abstract
- Several bird and fish heart mitochondrial cytochrome c oxidases have been isolated with a rapid and simple method involving hydrophobic and affinity chromatography. 2. Their spectrophotometric and kinetic properties are very similar to those of the mammalian enzymes. 3. These oxidases show a polypeptide composition simpler than the mammalian enzymes being composed of 9-10, instead of 13, different polypeptides. 4. These data suggest that the complexity of the mitochondrial heart oxidase increases with the stage of evolution.
摘要
- 已经通过一种涉及疏水色谱和亲和色谱的快速简单方法分离出了几种鸟类和鱼类心脏线粒体细胞色素c氧化酶。2. 它们的分光光度和动力学性质与哺乳动物的酶非常相似。3. 这些氧化酶的多肽组成比哺乳动物的酶更简单，由9 - 10种不同的多肽组成，而不是13种。4. 这些数据表明线粒体心脏氧化酶的复杂性随着进化阶段而增加。
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