Todd R D, Douglas M G
J Biol Chem. 1981 Jul 10;256(13):6984-9.
Monodisperse, Triton-solubilized ATPase complex was treated with the reversible protein-protein cross-linker dithiobis(succinimidyl)propionate under conditions where only intracomplex cross-links were formed. The resulting products were analyzed by two-dimensional sodium dodecyl sulfate-acrylamide slab gel electrophoresis under reducing and oxidizing conditions. Using the observed major subunit-subunit cross-links and the previously published subunit stoichiometries (Todd, R., Griesenbeck, T., and Douglas, M. (1980) J. Biol. Chem. 255, 5461-5467), a model of the ATPase complex was constructed. The model is a closed structure which could be formed by self-limited assembly of the subunits. The model also has the novel features of a pseudo-mirror symmetry and clustering of mitochondrially and nuclearly coded subunits into two different domains.
将单分散的、经曲拉通增溶的ATP酶复合物在仅形成复合物内交联的条件下，用可逆的蛋白质-蛋白质交联剂二硫代双（琥珀酰亚胺基）丙酸进行处理。在还原和氧化条件下，通过二维十二烷基硫酸钠-丙烯酰胺平板凝胶电泳对所得产物进行分析。利用观察到的主要亚基-亚基交联以及先前发表的亚基化学计量比（托德，R.，格里森贝克，T.，和道格拉斯，M.（1980年）《生物化学杂志》255卷，5461 - 5467页），构建了ATP酶复合物的模型。该模型是一个封闭结构，可通过亚基的自我限制组装形成。该模型还具有伪镜像对称以及线粒体编码亚基和核编码亚基聚集成两个不同结构域的新特征。
