从斑叶疆南星（Arum maculatum）线粒体中纯化F1 - ATP酶。与大鼠肝脏F1 - ATP酶亚基组成的比较。
Purification of F1-ATPase from cuckoo-pint (Arum maculatum) mitochondria. A comparison of subunit composition with that of rat liver F1-ATPase.
作者信息
Dunn P P, Slabas A R, Moore A L
出版信息
Biochem J. 1985 Feb 1;225(3):821-4. doi: 10.1042/bj2250821.
Plant mitochondrial ATPase has been chloroform-solubilized and purified by gel filtration from spadices of cuckoo-pint (Arum maculatum). The subunit composition of purified plant and rat liver ATPase were compared by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. The delta- and epsilon-subunits of the plant enzyme are larger than their supposed rat liver counterparts and, as such, A. maculatum mitochondrial ATPase shows structural homologies with the enzyme from Escherichia coli [Futai, Sternweis & Heppel (1974) Proc. Natl. Acad. Sci. U.S.A. 71, 2725-2729] rather than with the rat liver enzyme.
植物线粒体ATP酶已通过氯仿增溶，并从斑叶疆南星（Arum maculatum）的肉穗花序中经凝胶过滤纯化。通过十二烷基硫酸钠/聚丙烯酰胺凝胶电泳比较了纯化的植物和大鼠肝脏ATP酶的亚基组成。植物酶的δ亚基和ε亚基比其相应的大鼠肝脏亚基大，因此，斑叶疆南星线粒体ATP酶与大肠杆菌中的酶显示出结构同源性[Futai、Sternweis和Heppel（1974年），美国国家科学院院刊71，2725 - 2729]，而不是与大鼠肝脏酶。
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