Mullet J E, Pick U, Arntzen C J
Biochim Biophys Acta. 1981 Mar 20;642(1):149-57. doi: 10.1016/0005-2736(81)90145-0.
Negative staining of purified spinach dicyclohexylcarbodiimide (DCCD) sensitive ATPase revealed a population of 110 A subunits attached by stalks to short string-like aggregates. The interpretation of these data is that 110 A CF1 are attached by stalks to an aggregate of CF0. The CF1-CF0 complex was incorporated into phospholipid vesicles; freeze-fracture analysis of this preparation revealed a homogeneous population of particles spanning the lipid bilayer; those averaged 96 A in diameter. The DCCD binding proteolipid (apparent molecular weight 7500), an integral component of CF0, was isolated from membranes by butanol extraction and was incorporated into phospholipid vesicles. Freeze-fracture analysis of the DCCD-binding proteolipid/vesicle preparation revealed a population of particles averaging 83 A in diameter suggesting that the DCCD-binding proteolipid self-associates in lipid to form a stable complex. This complex may be required for proton transport across chloroplast membranes in vivo. The size difference between CF0 and DCCD-proteolipid freeze-fracture particles may be related to differences in polypeptide composition of the two complexes.
对纯化的菠菜二环己基碳二亚胺（DCCD）敏感ATP酶进行负染色，结果显示有一群110个A亚基通过柄与短串状聚集体相连。这些数据的解释是，110个A CF1通过柄与CF0的聚集体相连。CF1 - CF0复合物被整合到磷脂囊泡中；对该制剂的冷冻蚀刻分析显示，有一群均匀的颗粒横跨脂质双层；这些颗粒的平均直径为96埃。DCCD结合的质子转运膜内在蛋白（表观分子量7500）是CF0的一个组成部分，通过丁醇萃取从膜中分离出来，并被整合到磷脂囊泡中。对DCCD结合的质子转运膜内在蛋白/囊泡制剂的冷冻蚀刻分析显示，有一群平均直径为83埃的颗粒，这表明DCCD结合的质子转运膜内在蛋白在脂质中自缔合形成一个稳定的复合物。这种复合物可能是体内质子跨叶绿体膜运输所必需的。CF0和DCCD - 质子转运膜内在蛋白冷冻蚀刻颗粒之间的大小差异可能与这两种复合物的多肽组成差异有关。
