Roisin M P, Henry J P
Biochim Biophys Acta. 1982 Aug 20;681(2):292-9. doi: 10.1016/0005-2728(82)90034-2.
Ghosts derived from bovine chromaffin granules have a 32Pi-ATP exchange activity which is associated with the H+ pump of that membrane. This activity was low when compared to bacteria, chloroplasts or submitochondrial particles, but had similar properties (Km for ATP and Pi, ATP/Mg2+ ratio, pH profile, inhibition by dicyclohexylcarbodiimide and tributyltin) to the ATPase from above membranes. The 32Pi-ATP exchange activity was solubilized by cholate/octylglucoside mixtures. The soluble extract was lipid depleted by ammonium sulfate fractionation and partially purified by sucrose gradient centrifugation. The purified preparation was reconstituted with phospholipids by freeze-thawing. The reconstituted vesicles had a 32Pi-ATP exchange sensitive to dicyclohexylcarbodiimide and trybutyltin and an ATPase with a sensitivity to the inhibitors which varied with the reconstitution conditions. The alpha- and beta-subunits of F1-ATPase were major components of the preparation.
源自牛嗜铬粒的囊泡具有32Pi-ATP交换活性，该活性与该膜的H+泵相关。与细菌、叶绿体或亚线粒体颗粒相比，这种活性较低，但具有与上述膜的ATP酶相似的性质（ATP和Pi的Km值、ATP/Mg2+比率、pH曲线、二环己基碳二亚胺和三丁基锡的抑制作用）。32Pi-ATP交换活性可被胆酸盐/辛基葡糖苷混合物溶解。通过硫酸铵分级分离使可溶性提取物脱脂，并通过蔗糖梯度离心进行部分纯化。通过冻融法用磷脂重构纯化的制剂。重构的囊泡具有对二环己基碳二亚胺和三丁基锡敏感的32Pi-ATP交换以及对抑制剂敏感的ATP酶，其敏感性随重构条件而变化。F1-ATP酶的α和β亚基是该制剂的主要成分。
