大肠杆菌膜泡的异质性及其用ATP酶抗体进行的亚分级分离。
Heterogeneity of membrane vesicles from Escherichia coli and their subfractionation with antibody to ATPase.
作者信息
Hare J F, Olden K, Kennedy E P
出版信息
Proc Natl Acad Sci U S A. 1974 Dec;71(12):4843-6. doi: 10.1073/pnas.71.12.4843.
Abstract
The energy-transducing, Mg-Ca activated ATPase (ATP phosphohydrolase, EC 3.6.1.3) of E. coli is located on the inner surface of the cytoplasmic membrane. Antibody to purified ATPase has now been used to demonstrate that membrane vesicles as ordinarily prepared by the lysozyme-EDTA method consist of two distinct populations. About half the vesicles are everted, and thus readily agglutinated by antibody to ATPase, while half are right-side out. NADH oxidase (reduced NAD:O(2) oxidoreductase EC 1.6.99.3) activity is associated almost entirely with everted vesicles, while the ability to concentrate proline is a property of the right-side out vesicles. The results explain the failure of previous workers to observe the energization of membrane vesicles by oxidation of NADH.
摘要
大肠杆菌的能量转换型镁钙激活ATP酶（ATP磷酸水解酶，EC 3.6.1.3）位于细胞质膜的内表面。现已使用针对纯化ATP酶的抗体来证明，通常通过溶菌酶-乙二胺四乙酸方法制备的膜囊泡由两个不同的群体组成。大约一半的囊泡是外翻的，因此很容易被ATP酶抗体凝集，而另一半是正常取向的。NADH氧化酶（还原型NAD：O₂氧化还原酶，EC 1.6.99.3）活性几乎完全与外翻囊泡相关，而浓缩脯氨酸的能力是正常取向囊泡的特性。这些结果解释了先前研究人员未能观察到通过NADH氧化使膜囊泡产生能量的原因。
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