期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1974
卷号：71
期号：12
页码：4843-4846
DOI：10.1073/pnas.71.12.4843
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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:O2 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.
关键词：membrane transport ; bioenergetics ; NADH oxidase ; D-lactate dehydrogenase
