Cidon S, Nelson N
J Biol Chem. 1983 Mar 10;258(5):2892-98.
The ATPase activity of the chromaffin granule membrane was found to differ profoundly from that of the mitochondrial inner membrane. First, mitochondrial ATPase is much more sensitive to low concentrations of dicyclohexylcarbodiimide than the chromaffin granule ATPase. Second, analysis of chromaffin granule preparations by immune replication revealed that mitochondrial contamination (as measured with an antibody against cytochrome c oxidase) could account for the presence of mitochondrial-type ATPase. Third, exposure of chromaffin granule preparation to sodium bromide removed the mitochondrial-type ATPase, but left over 70% of the total ATPase activity of the chromaffin granules intact. Finally, after solubilization of the chromaffin granule membranes with detergents, a novel ATPase could be separated from the mitochondrial-type ATPase. It is proposed that this novel ATPase represents most of the ATPase activity of the chromaffin granules and that the mitochondrial-type ATPase reflects contamination by mitochondria.
已发现嗜铬粒细胞膜的ATP酶活性与线粒体内膜的ATP酶活性有很大差异。首先，线粒体ATP酶比嗜铬粒ATP酶对低浓度的二环己基碳二亚胺更为敏感。其次，通过免疫复制对嗜铬粒制剂进行分析发现，线粒体污染（用抗细胞色素c氧化酶抗体测量）可解释线粒体型ATP酶的存在。第三，将嗜铬粒制剂暴露于溴化钠中可去除线粒体型ATP酶，但嗜铬粒总ATP酶活性仍有70%以上保持完整。最后，在用去污剂溶解嗜铬粒细胞膜后，可将一种新型ATP酶与线粒体型ATP酶分离。有人提出，这种新型ATP酶代表了嗜铬粒的大部分ATP酶活性，而线粒体型ATP酶反映了线粒体的污染。
