Penin F, Deléage G, Gagliardi D, Roux B, Gautheron D C
Laboratoire de Biologie et Technologie des Membranes du CNRS, Université Claude Bernard de Lyon, Villeurbanne, France.
Biochemistry. 1990 Oct 9;29(40):9358-64. doi: 10.1021/bi00492a008.
A delta epsilon complex has been purified as a molecular entity from pig heart mitochondrial F1-ATPase. This delta epsilon complex has also been reconstituted from purified delta and epsilon subunits. Both isolated and reconstituted delta epsilon complexes have delta 1 epsilon 1 stoichiometry and are indistinguishable by their chromatographic behavior, their circular dichroism spectra (CD spectra), and their intrinsic fluorescence features. The content of secondary structures deduced from CD spectra of the delta epsilon complex appears to be the sum of the respective contributions of purified delta and epsilon subunits. All intrinsic fluorescence studies carried out on isolated epsilon subunit and delta epsilon complex show that the single tryptophan residue located on epsilon is involved in the interaction between delta and epsilon subunits. Results obtained with F1-ATPase are in favor of the same delta epsilon interaction in the entire enzyme.
一种δε复合物已作为一种分子实体从猪心脏线粒体F1 - ATP酶中纯化出来。这种δε复合物也已由纯化的δ和ε亚基重构而成。分离得到的和重构的δε复合物均具有δ1ε1化学计量比，并且在色谱行为、圆二色光谱（CD光谱）以及固有荧光特征方面无法区分。从δε复合物的CD光谱推导得出的二级结构含量似乎是纯化的δ和ε亚基各自贡献的总和。对分离出的ε亚基和δε复合物进行的所有固有荧光研究表明，位于ε上的单个色氨酸残基参与了δ和ε亚基之间的相互作用。用F1 - ATP酶获得的结果支持在整个酶中存在相同的δε相互作用。
