从红螺菌的ATP合酶中分离并鉴定一种功能性αβ异二聚体。
Isolation and characterisation of a functional alpha beta heterodimer from the ATP synthase of Rhodospirillum rubrum.
作者信息
Andralojc P J, Harris D A
机构信息
Department of Biochemistry, University of Oxford, UK.
出版信息
FEBS Lett. 1992 Sep 28;310(2):187-92. doi: 10.1016/0014-5793(92)81326-h.
An alpha beta heterodimer of the F1-ATPase of Rhodospirillum rubrum was isolated by extraction of chromatophores with LiCl. Each alpha beta heterodimer contains one tightly bound ADP, which is released upon removal of medium Mg2+. The dimer can be reversibly dissociated by removal of Mg(2+)-ions. The alpha beta heterodimer restores both ATP-synthetic and -hydrolytic activities to LiCl-treated chromatophores, saturation being achieved at approximately 2 mmol alpha beta.mol BChl-1. The heterodimer itself hydrolyses Mg-ATP with an activity distinct from RF1, being unaffected by azide or sulphite ions. The Vmax and Km (ATP) for this Mg(2+)-dependent activity were 110 +/- 10 nmol.min-1.mg protein-1 and 100 +/- 30 microM, respectively. The Km did not differ significantly from that of RF1.
通过用LiCl提取载色体，分离出了红螺菌F1 - ATP酶的αβ异二聚体。每个αβ异二聚体含有一个紧密结合的ADP，在去除培养基中的Mg2+后会释放出来。通过去除Mg(2+)离子，二聚体可以可逆解离。αβ异二聚体可将ATP合成和水解活性恢复到LiCl处理的载色体中，在约2 mmol αβ.mol BChl-1时达到饱和。该异二聚体本身水解Mg - ATP的活性不同于RF1，不受叠氮化物或亚硫酸根离子的影响。这种Mg(2+)依赖性活性的Vmax和Km（ATP）分别为110±10 nmol·min-1·mg蛋白-1和100±30 μM。Km与RF1的Km没有显著差异。
Zotero 插件