Inhibitory effect of duramycin on partial reactions catalyzed by (Na+,K+)-adenosinetriphosphatase from dog kidney.
Inhibitory effect of duramycin on partial reactions catalyzed by (Na+,K+)-adenosinetriphosphatase from dog kidney.
复制标题
耐久霉素对犬肾(Na,K)-三磷酸腺苷酶催化部分反应的抑制作用。
DOI：
10.1021/bi00297a031
复制
发表时间：
1984
期刊：
影响因子：
2.9
通讯作者：
Racker,E
中科院分区：
文献类型：
--
作者：
Nakamura,S;Racker,E
磷脂可能是其作用方式的线索。当以低浓度（5 pg/mg脂质）加入持续霉素时，Asolectin、PE和PS（但不是PC囊泡）变得浑浊。该结果表明，耐久霉素直接与某些磷脂相互作用。狗肾（Na+，K+）-ATP酶的敏感性明显高于膜制剂。因此，尚不清楚抑制剂是否直接与蛋白质相互作用或是否干扰特定的蛋白质-脂质相互作用。耐久霉素抑制网格蛋白包被囊泡和质膜的ATP酶活性。它对肌浆网的Ca 2 +-ATP酶几乎没有影响，并且即使在非常高的浓度下也对牛心脏线粒体的F1-ATP酶没有影响（Stone等人，1984; Racker等人，1984年）。然而，它在高浓度下抑制牛心脏亚线粒体颗粒的ATP酶活性。F [和亚线粒体颗粒之间易感性的差异可能是由于酶与抑制性蛋白的奇怪结合以及磷脂对其的逆转（Bulos & Racker，1968）。因此，duramycin对线粒体ATP酶的抑制作用可能与寡霉素相似。因此，耐久霉素和脂质之间的相互作用的显着的特异性可能有助于进一步探索脂质-蛋白质相互作用。
phospholipids may be a clue to its mode of action. Asolectin, PE, and PS, but not PC vesicles, became turbid when duramycin was added at low concentrations (5 pg/mg of lipid). This result suggests that duramycin directly interacts with some phospholipids. The lubrol-solubilized dog kidney (Na+, K+)-ATPase was much more sensitive than the mem-branous preparation. It is therefore not clear whether the inhibitor interacts directly with the protein or whether it interferes with a specific protein-lipid interaction. Duramycin inhibits the ATPase activity of clathrin-coated vesicles and of plasma membranes. It has little effect on the Ca2+-ATPase of sarcoplasmic reticulum and none on the F,-ATPase of bovine heart mitochondria even at very high concentrations (Stone et al., 1984; Racker et al., 1984). It does, however, inhibit at high concentrations the ATPase activity of submitochondrial particles from bovine heart. The difference in susceptibility between F [and submitochondrial particles may be due tothe curious association of the enzyme with an inhibitory mitochondrialprotein and its reversal by phospholipids (Bulos & Racker, 1968). Thus, duramycin may have an inhibitory effect on mitochondrial ATPase similar to that of oligomycin. The remarkable specificity of the inter-action between duramycin and lipids may therefore lend itself to further explorations of lipid-protein interactions.